{ "ProductData": { "ID": "CPS_000031", "ProductType": "Others", "BrandName": "AMYL2", "ProductNameAddition": "α-Amylase EPS ver.2", "RegulatoryDisclaimer1": "For in vitro diagnostic use.", "DisclaimerGroup1": "IVD", "RegulatoryDisclaimer2": null, "DisclaimerGroup2": null, "RegulatoryDisclaimer3": null, "SampleType": [ "EDTA plasma", "Plasma", "Serum", "Urine" ], "LicenseDisclaimers": [ ], "RelatedLinks": "", "Clone": "", "ControlTissue": [ "" ], "ISOtypes": "", "Species": [ "" ], "StainLocalization": [ "" ], "ProductNameGlobal": "AMYL2" }, "ProductImageDetails": { "ImagePath": "https://pim-media.roche.com/Images/Article_05401496190_im_en.png", "ImageType": "Image main" }, "Product2Taxonomy": { "Product2TaxonomyReferences": [ { "StructureSystemIdentifier": "Product_Grouping", "StructureSystemName": "Product Grouping", "NodeID": "01-0334", "StructureNodeStatus": "Active", "NodeName": "cobas Amylase–total" }, { "StructureSystemIdentifier": "OWP_Product_Types", "StructureSystemName": "Product Types", "NodeID": "20-000-00", "StructureNodeStatus": "Active", "NodeName": "Assays Reagents and Strips" }, { "StructureSystemIdentifier": "Lab_Type", "StructureSystemName": "Lab Types", "NodeID": "050-00", "StructureNodeStatus": "Active", "NodeName": "Core Lab" }, { "StructureSystemIdentifier": "Health_Topics", "StructureSystemName": "Health Topics", "NodeID": "12-00-00", "StructureNodeStatus": "Active", "NodeName": "Endocrinology" }, { "StructureSystemIdentifier": "Product_Solutions", "StructureSystemName": "Product Solutions", "NodeID": "020", "StructureNodeStatus": "Active", "NodeName": "Clinical Chemistry" }, { "StructureSystemIdentifier": "Applications", "StructureSystemName": "Applications", "NodeID": "99-00-00", "StructureNodeStatus": "Inactive", "NodeName": "" }, { "StructureSystemIdentifier": "OWP_Techniques", "StructureSystemName": "Techniques", "NodeID": "999-00", "StructureNodeStatus": "Inactive", "NodeName": "" }, { "StructureSystemIdentifier": "Pathogens", "StructureSystemName": "Pathogens", "NodeID": "99-00-00", "StructureNodeStatus": "Inactive", "NodeName": "" }, { "StructureSystemIdentifier": "Disease_Areas", "StructureSystemName": "Disease Areas", "NodeID": "99-00-00", "StructureNodeStatus": "Inactive", "NodeName": "" }, { "StructureSystemIdentifier": "Indications", "StructureSystemName": "Indications", "NodeID": "97", "StructureNodeStatus": "Active", "NodeName": "Endocrinology" }, { "StructureSystemIdentifier": "OWP_Family", "StructureSystemName": "Product Families", "NodeID": "622", "StructureNodeStatus": "Active", "NodeName": "COBAS INTEGRA" } ] }, "Product2Materials": { "P2MaterialReferences": [ { "MaterialNum": "05167027214", "MaterialDescription": "AMYL Gen.2, 750Tests cobas c701", "RegisteredProductName": "AMYL2", "GTIN": "07613336161616", "ProductCategoryText": "Reagents, kits", "OldMaterialNumber": "", "PackSizePIM360": "750 tests", "PackSizeDescPIM360": "cobas c 701/702", "MaterialAnnotation": "", "ReadyForUse": "true", "OrderInformation": "" }, { "MaterialNum": "05167027519", "MaterialDescription": "AMYL Gen.2, 750Tests cobas c701", "RegisteredProductName": "AMYL2", "GTIN": "", "ProductCategoryText": "Reagents, kits", "OldMaterialNumber": "", "PackSizePIM360": "750 tests", "PackSizeDescPIM360": "cobas c 701/702", "MaterialAnnotation": "", "ReadyForUse": "", "OrderInformation": "" }, { "MaterialNum": "05401496190", "MaterialDescription": "a-Amylase 200T cobas c 111", "RegisteredProductName": "AMYL2", "GTIN": "04015630926886", "ProductCategoryText": "Reagents, kits", "OldMaterialNumber": "", "PackSizePIM360": "2 × 100 tests", "PackSizeDescPIM360": "cobas c 111", "MaterialAnnotation": "", "ReadyForUse": "true", "OrderInformation": "" }, { "MaterialNum": "08056811190", "MaterialDescription": "AMYL2, 750T, cobas c pack green", "RegisteredProductName": "AMYL2", "GTIN": "07613336121009", "ProductCategoryText": "Reagents, kits", "OldMaterialNumber": "", "PackSizePIM360": "750 tests", "PackSizeDescPIM360": "cobas c 303/503", "MaterialAnnotation": "", "ReadyForUse": "true", "OrderInformation": "" }, { "MaterialNum": "03183742122", "MaterialDescription": "AMYL Gen.2, 300Tests, cobas c, Integra", "RegisteredProductName": "AMYL2", "GTIN": "04015630918935", "ProductCategoryText": "Reagents, kits", "OldMaterialNumber": "0766097", "PackSizePIM360": "300 tests", "PackSizeDescPIM360": "COBAS INTEGRA 400 Plus, cobas c 311/501/502", "MaterialAnnotation": "", "ReadyForUse": "true", "OrderInformation": "" }, { "MaterialNum": "05167027190", "MaterialDescription": "AMYL Gen.2, 750Tests cobas c701", "RegisteredProductName": "AMYL2", "GTIN": "04015630924875", "ProductCategoryText": "Reagents, kits", "OldMaterialNumber": "", "PackSizePIM360": "750 tests", "PackSizeDescPIM360": "cobas c 701/702", "MaterialAnnotation": "", "ReadyForUse": "true", "OrderInformation": "" }, { "MaterialNum": "05167027188", "MaterialDescription": "AMYL Gen.2, 750Tests cobas c701", "RegisteredProductName": "AMYL2", "GTIN": "07613336161609", "ProductCategoryText": "Reagents, kits", "OldMaterialNumber": "", "PackSizePIM360": "750 tests", "PackSizeDescPIM360": "cobas c 701/702", "MaterialAnnotation": "", "ReadyForUse": "true", "OrderInformation": "" } ] }, "Product2Products": { "Product2ProductReference": [ { "ProductID": "INS_2113", "BrandName": "cobas® c 502 module", "ProductNameAddition": "", "ReferenceType": "Instrument", "Classification": [ { "IdentifierofStructureSystem": "1", "NameofStructureSystem": "GPCH", "StructureNodeID": "2324", "StructureGroupPath": "ClinChem fully automated->Systems / Digital Products->cobas c systems->cobas c 502", "StructureGroupName": "cobas c 502", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Product_Types", "NameofStructureSystem": "Product Types", "StructureNodeID": "10-000-00", "StructureGroupPath": "Analyzer Instruments and Systems", "StructureGroupName": "Analyzer Instruments and Systems", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "050-00", "StructureGroupPath": "Core Lab", "StructureGroupName": "Core Lab", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Product_Solutions", "NameofStructureSystem": "Product Solutions", "StructureNodeID": "020", "StructureGroupPath": "Clinical Chemistry", "StructureGroupName": "Clinical Chemistry", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Applications", "NameofStructureSystem": "Applications", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Techniques", "NameofStructureSystem": "Techniques", "StructureNodeID": "999-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Disease_Areas", "NameofStructureSystem": "Disease Areas", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Pathogens", "NameofStructureSystem": "Pathogens", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Health_Topics", "NameofStructureSystem": "Health Topics", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "614", "StructureGroupPath": "cobas c", "StructureGroupName": "cobas c", "StructureNodeStatus": "Active" } ] }, { "ProductID": "INS_6347", "BrandName": "cobas® c 303 analytical unit", "ProductNameAddition": "", "ReferenceType": "Instrument", "Classification": [ { "IdentifierofStructureSystem": "1", "NameofStructureSystem": "GPCH", "StructureNodeID": "9493", "StructureGroupPath": "ClinChem fully automated->Systems / Digital Products->cobas c systems->cobas c 303", "StructureGroupName": "cobas c 303", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Product_Types", "NameofStructureSystem": "Product Types", "StructureNodeID": "10-000-00", "StructureGroupPath": "Analyzer Instruments and Systems", "StructureGroupName": "Analyzer Instruments and Systems", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "050-00", "StructureGroupPath": "Core Lab", "StructureGroupName": "Core Lab", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Product_Solutions", "NameofStructureSystem": "Product Solutions", "StructureNodeID": "020", "StructureGroupPath": "Clinical Chemistry", "StructureGroupName": "Clinical Chemistry", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Applications", "NameofStructureSystem": "Applications", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Techniques", "NameofStructureSystem": "Techniques", "StructureNodeID": "999-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Disease_Areas", "NameofStructureSystem": "Disease Areas", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Pathogens", "NameofStructureSystem": "Pathogens", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Health_Topics", "NameofStructureSystem": "Health Topics", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "614", "StructureGroupPath": "cobas c", "StructureGroupName": "cobas c", "StructureNodeStatus": "Active" } ] }, { "ProductID": "INS_2177", "BrandName": "cobas® c 702 module", "ProductNameAddition": "", "ReferenceType": "Instrument", "Classification": [ { "IdentifierofStructureSystem": "1", "NameofStructureSystem": "GPCH", "StructureNodeID": "2492", "StructureGroupPath": "ClinChem fully automated->Systems / Digital Products->cobas c systems->cobas c 702", "StructureGroupName": "cobas c 702", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Product_Types", "NameofStructureSystem": "Product Types", "StructureNodeID": "10-000-00", "StructureGroupPath": "Analyzer Instruments and Systems", "StructureGroupName": "Analyzer Instruments and Systems", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "050-00", "StructureGroupPath": "Core Lab", "StructureGroupName": "Core Lab", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Product_Solutions", "NameofStructureSystem": "Product Solutions", "StructureNodeID": "020", "StructureGroupPath": "Clinical Chemistry", "StructureGroupName": "Clinical Chemistry", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Applications", "NameofStructureSystem": "Applications", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Techniques", "NameofStructureSystem": "Techniques", "StructureNodeID": "999-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Disease_Areas", "NameofStructureSystem": "Disease Areas", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Pathogens", "NameofStructureSystem": "Pathogens", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Health_Topics", "NameofStructureSystem": "Health Topics", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "614", "StructureGroupPath": "cobas c", "StructureGroupName": "cobas c", "StructureNodeStatus": "Active" } ] }, { "ProductID": "INS_501", "BrandName": "cobas® c 701 module", "ProductNameAddition": "", "ReferenceType": "Instrument", "Classification": [ { "IdentifierofStructureSystem": "1", "NameofStructureSystem": "GPCH", "StructureNodeID": "310", "StructureGroupPath": "ClinChem fully automated->Systems / Digital Products->cobas c systems->cobas c 701", "StructureGroupName": "cobas c 701", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Product_Types", "NameofStructureSystem": "Product Types", "StructureNodeID": "10-000-00", "StructureGroupPath": "Analyzer Instruments and Systems", "StructureGroupName": "Analyzer Instruments and Systems", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "050-00", "StructureGroupPath": "Core Lab", "StructureGroupName": "Core Lab", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Product_Solutions", "NameofStructureSystem": "Product Solutions", "StructureNodeID": "020", "StructureGroupPath": "Clinical Chemistry", "StructureGroupName": "Clinical Chemistry", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Applications", "NameofStructureSystem": "Applications", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Techniques", "NameofStructureSystem": "Techniques", "StructureNodeID": "999-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Disease_Areas", "NameofStructureSystem": "Disease Areas", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Pathogens", "NameofStructureSystem": "Pathogens", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Health_Topics", "NameofStructureSystem": "Health Topics", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "614", "StructureGroupPath": "cobas c", "StructureGroupName": "cobas c", "StructureNodeStatus": "Active" } ] }, { "ProductID": "INS_338", "BrandName": "cobas® c 501 module", "ProductNameAddition": "", "ReferenceType": "Instrument", "Classification": [ { "IdentifierofStructureSystem": "1", "NameofStructureSystem": "GPCH", "StructureNodeID": "309", "StructureGroupPath": "ClinChem fully automated->Systems / Digital Products->cobas c systems->cobas c 501", "StructureGroupName": "cobas c 501", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Product_Types", "NameofStructureSystem": "Product Types", "StructureNodeID": "10-000-00", "StructureGroupPath": "Analyzer Instruments and Systems", "StructureGroupName": "Analyzer Instruments and Systems", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "050-00", "StructureGroupPath": "Core Lab", "StructureGroupName": "Core Lab", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Product_Solutions", "NameofStructureSystem": "Product Solutions", "StructureNodeID": "020", "StructureGroupPath": "Clinical Chemistry", "StructureGroupName": "Clinical Chemistry", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Applications", "NameofStructureSystem": "Applications", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Techniques", "NameofStructureSystem": "Techniques", "StructureNodeID": "999-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Disease_Areas", "NameofStructureSystem": "Disease Areas", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Pathogens", "NameofStructureSystem": "Pathogens", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Health_Topics", "NameofStructureSystem": "Health Topics", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "614", "StructureGroupPath": "cobas c", "StructureGroupName": "cobas c", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "679", "StructureGroupPath": "cobas 6000", "StructureGroupName": "cobas 6000", "StructureNodeStatus": "Active" } ] }, { "ProductID": "INS_2043", "BrandName": "cobas® c 311 analyzer", "ProductNameAddition": "", "ReferenceType": "Instrument", "Classification": [ { "IdentifierofStructureSystem": "1", "NameofStructureSystem": "GPCH", "StructureNodeID": "308", "StructureGroupPath": "ClinChem fully automated->Systems / Digital Products->cobas c systems->cobas c 311", "StructureGroupName": "cobas c 311", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Product_Types", "NameofStructureSystem": "Product Types", "StructureNodeID": "10-000-00", "StructureGroupPath": "Analyzer Instruments and Systems", "StructureGroupName": "Analyzer Instruments and Systems", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "050-00", "StructureGroupPath": "Core Lab", "StructureGroupName": "Core Lab", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Product_Solutions", "NameofStructureSystem": "Product Solutions", "StructureNodeID": "020", "StructureGroupPath": "Clinical Chemistry", "StructureGroupName": "Clinical Chemistry", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Applications", "NameofStructureSystem": "Applications", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Techniques", "NameofStructureSystem": "Techniques", "StructureNodeID": "999-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Disease_Areas", "NameofStructureSystem": "Disease Areas", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Pathogens", "NameofStructureSystem": "Pathogens", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Health_Topics", "NameofStructureSystem": "Health Topics", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "614", "StructureGroupPath": "cobas c", "StructureGroupName": "cobas c", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "560", "StructureGroupPath": "cobas 4000", "StructureGroupName": "cobas 4000", "StructureNodeStatus": "Active" } ] }, { "ProductID": "INS_526", "BrandName": "cobas® c 111 analyzer", "ProductNameAddition": "", "ReferenceType": "Instrument", "Classification": [ { "IdentifierofStructureSystem": "1", "NameofStructureSystem": "GPCH", "StructureNodeID": "307", "StructureGroupPath": "ClinChem fully automated->Systems / Digital Products->cobas c systems->cobas c 111", "StructureGroupName": "cobas c 111", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Product_Types", "NameofStructureSystem": "Product Types", "StructureNodeID": "10-000-00", "StructureGroupPath": "Analyzer Instruments and Systems", "StructureGroupName": "Analyzer Instruments and Systems", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "050-00", "StructureGroupPath": "Core Lab", "StructureGroupName": "Core Lab", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Lab_Type", "NameofStructureSystem": "Lab Types", "StructureNodeID": "110-00", "StructureGroupPath": "Point of Care Testing", "StructureGroupName": "Point of Care Testing", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Product_Solutions", "NameofStructureSystem": "Product Solutions", "StructureNodeID": "020", "StructureGroupPath": "Clinical Chemistry", "StructureGroupName": "Clinical Chemistry", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "Applications", "NameofStructureSystem": "Applications", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "OWP_Techniques", "NameofStructureSystem": "Techniques", "StructureNodeID": "999-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Disease_Areas", "NameofStructureSystem": "Disease Areas", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Pathogens", "NameofStructureSystem": "Pathogens", "StructureNodeID": "99-00-00", "StructureGroupPath": "", "StructureGroupName": "", "StructureNodeStatus": "Inactive" }, { "IdentifierofStructureSystem": "Health_Topics", "NameofStructureSystem": "Health Topics", "StructureNodeID": "11-00-00", "StructureGroupPath": "Critical Care", "StructureGroupName": "Critical Care", "StructureNodeStatus": "Active" }, { "IdentifierofStructureSystem": "OWP_Family", "NameofStructureSystem": "Product Families", "StructureNodeID": "614", "StructureGroupPath": "cobas c", "StructureGroupName": "cobas c", "StructureNodeStatus": "Active" } ] } ] }, "ProductSpec": [ { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "0005167027190c701", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "8", "DocumentObjectID": "FF0000000487610E", "DocumentOriginID": "FF000000030F040E", "MaterialNumbers": [ "05167027190", "05167027214" ], "InstrumentReferences": [ { "ID": "2492", "BrandName": "cobas c 702" }, { "ID": "310", "BrandName": "cobas c 701" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "

Intended use

In vitro test for the quantitative determination of α‑amylase in human serum, plasma and urine on Roche/Hitachi cobas c systems.

", "Language": "en" }, { "Name": "TestPrinciple", "Value": "

Test principle

Test principle
LREFLorentz K. Approved recommendation on IFCC methods for the measurement of catalytic concentration of enzymes. Part 9. IFCC Method for α-Amylase. (1,4-α-D-Glucan 4-Glucanohydrolase, EC 3.2.1.1). Clin Chem Lab Med 1998;36(3):185-203.
,
LREFKurrle-Weitenhiller A, Hölzel W, Engel D, et al. Method for the determination of total and pancreatic α-amylase based on 100 % cleavage of the protected substrate ethylidene-4-nitrophenyl-maltoheptaoside. Clin Chem 1996;42(S6):98.

Enzymatic colorimetric assay acc. to IFCC.

Defined oligosaccharides such as 4,6‑ethylidene‑(G7)‑ p‑nitrophenyl‑(G1)‑α,D‑maltoheptaoside (ethylidene‑G7PNP)a) are cleaved under the catalytic action of α‑amylases. The G2PNP, G3PNP and G4PNP fragments so formed are completely hydrolyzed to p‑nitrophenol and glucose by α‑glucosidase.

Simplified reaction scheme:

α‑amylase

5 ethylidene‑G7PNP + 5 H2O

2 ethylidene‑G5 + 2 G2PNP + 2 ethylidene‑G4 + 2 G3PNP
+ ethylidene‑G3 + G4PNP

α‑glucosidase

2 G2PNP + 2 G3PNP + G4PNP + 14 H2O

5 PNP + 14 Gb)

a) PNP p‑nitrophenol
b) G Glucose

The color intensity of the p‑nitrophenol formed is directly proportional to the α‑amylase activity. It is determined by measuring the increase in absorbance.

", "Language": "en" }, { "Name": "MeasuringRange", "Value": "

Limits and ranges

Measuring range

Serum/plasma/urine

3‑1500 U/L (0.05‑25.0 µkat/L)

Determine samples having higher activities via the rerun function. Dilution of samples via the rerun function is a 1:5 dilution. Results from samples diluted using the rerun function are automatically multiplied by a factor of 5.

Lower limits of measurement

Lower detection limit:

3 U/L (0.05 µkat/L)

The lower detection limit represents the lowest measurable analyte level that can be distinguished from zero. It is calculated as the value lying 3 standard deviations above that of the lowest standard (standard 1 + 3 SD, repeatability, n = 21).

Values below the lower detection limit (< 3 U/L) will not be flagged by the instrument.

", "Language": "en" }, { "Name": "ExpectedValues", "Value": "

Expected values

Expected values
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC Clin Biochem/Erratum. Clin Biochem 2003;36:161.

Serum/plasma

Men/Women

0.47‑1.67 µkat/L

28‑100 U/L

Spontaneously voided urine

Men
Women

0.27‑8.20 µkat/L
0.35‑7.46 µkat/L

16‑491 U/L
21‑447 U/L

α‑amylase/
creatinine quotient

Men
Women

0.97‑4.73 µkat/g
1.25‑6.51 µkat/g

58‑283 U/g
75‑390 U/g

α‑Amylase/creatinine quotient

To allow for fluctuations in the α‑amylase activity in urine, it is advisable to determine the α‑amylase/creatinine quotient. To do this, determine the α‑amylase activity and creatinine concentration in spontaneously voided urine.

Quotient [U/g or µkat/mmol]

=

α‑amylase [U/L or µkat/L]

creatinine [g/L or mmol/L]

Amylase/Creatinine Clearance Ratio (ACCR)

LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press, 1997, 2nd edition.

The ACCR is calculated from amylase activity and creatinine concentration. Both the serum and urine samples should be collected at the same time.

ACCR [%] =

urine amylase [U/L] × serum creatinine [mg/L]

× 100

serum amylase [U/L] × urine creatinine [mg/L]

The ACCR is approximately equal to 2‑5 %.

Each laboratory should investigate the transferability of the expected values to its own patient population and if necessary determine its own reference ranges.

", "Language": "en" }, { "Name": "LimitationInterference", "Value": "

Limitations - interference

A slight change in the yellow coloration of solution 2 does not interfere with the performance of the test.

Do not pipette by mouth, and ensure that the reagent does not come into contact with the skin. Saliva and sweat contain α‑amylase!

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 100 U/L (1.67 µkat/L).

Serum/plasma

Icterus:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an I index of 60 for conjugated and unconjugated bilirubin (approximate conjugated and unconjugated bilirubin concentration: 1026 µmol/L or 60 mg/dL).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Lipemia (Intralipid):

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an L index of 1500. There is poor correlation between the L index (corresponds to turbidity) and triglycerides concentration.

In rare cases, samples with a combination of elevated turbidity (L‑index) and high Amylase activity may cause a >React or >Abs flag.

Highly turbid and grossly lipemic samples may cause Abs. flags.

Anticoagulants: Interference was found with citrate, fluoride, and EDTA.

LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press, 1997, 2nd edition.

Glucose: No significant interference from glucose up to a concentration of 111 mmol/L (2000 mg/dL). Approximately 10 % higher recovery was found at glucose concentrations of 250 mmol/L (4500 mg/dL).

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 5.68 mmol/L (100 mg/dL).

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFBreuer J. Report on the Symposium "Drug effects in Clinical Chemistry Methods". Eur J Clin Chem Clin Biochem 1996;34:385-386.
,
LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Exception:

LREFGokal R, Moberly J, Lindholm B, et al. Metabolic and laboratory effects of icodextrin. Kidney Int 2002;62(81):62-71.
Icodextrin-based drugs may lead to decreased amylase results.

In very rare cases, gammopathy, in particular type IgM (Waldenström’s macroglobulinemia), may cause unreliable results.

LREFBakker AJ, Mücke M. Gammopathy interference in clinical chemistry assays: mechanisms, detection and prevention. Clin Chem Lab Med 2007;45(9):1240-1243.

Urine

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 2.27 mmol/L (40 mg/dL). Approximately 15 % lower recovery was found at ascorbic acid concentrations of 22.7 mmol/L (400 mg/dL).

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 460 U/L (7.68 µkat/L).

Hemolysis: No significant interference up to a hemoglobin concentration of 311 µmol/L or 500 mg/dL.

Phosphate: No significant interference from phosphate up to a concentration of 70 mmol/L (217 mg/dL).

Urea: No significant interference from urea up to a concentration of 1500 mmol/L (9009 mg/dL).

For diagnostic purposes, the results should always be assessed in conjunction with the patient’s medical history, clinical examination and other findings.

ACTION REQUIRED
Special Wash Programming: The use of special wash steps is mandatory when certain test combinations are run together on Roche/Hitachi cobas c systems. All special wash programming necessary for avoiding carry‑over is available via the cobas link, manual input is required in certain cases. The latest version of the carry‑over evasion list can be found with the NaOHD/SMS/SmpCln1+2/SCCS Method Sheet and for further instructions refer to the operator’s manual.

Where required, special wash/carry‑over evasion programming must be implemented prior to reporting results with this test.

", "Language": "en" }, { "Name": "OrderInformation", "Value": "

OrderInformation (CC Reagents - cobas + Integra)

Order information

Analyzer(s) on which cobas c pack(s) can be used

05167027 190*

α‑Amylase EPS ver.2 (750 tests)

System‑ID 05 6609 7

Roche/Hitachi cobas c 701/702

05167027 214*

α‑Amylase EPS ver.2 (750 tests)

System‑ID 05 6609 7

Roche/Hitachi cobas c 701/702

Materials required (but not provided):

10759350 190

Calibrator f.a.s. (12 x 3 mL)

Code 401

10759350 360

Calibrator f.a.s. (12 x 3 mL, for USA)

Code 401

12149435 122

Precinorm U plus (10 x 3 mL)

Code 300

12149435 160

Precinorm U plus (10 x 3 mL, for USA)

Code 300

12149443 122

Precipath U plus (10 x 3 mL)

Code 301

12149443 160

Precipath U plus (10 x 3 mL, for USA)

Code 301

05117003 190

PreciControl ClinChem Multi 1 (20 x 5 mL)

Code 391

05947626 190

PreciControl ClinChem Multi 1 (4 x 5 mL)

Code 391

05947626 160

PreciControl ClinChem Multi 1 (4 x 5 mL, for USA)

Code 391

05117216 190

PreciControl ClinChem Multi 2 (20 x 5 mL)

Code 392

05947774 190

PreciControl ClinChem Multi 2 (4 x 5 mL)

Code 392

05947774 160

PreciControl ClinChem Multi 2 (4 x 5 mL, for USA)

Code 392

05172152 190

Diluent NaCl 9 % (119 mL)

System‑ID 08 6869 3

* Some kits shown may not be available in all countries.

", "Language": "en" }, { "Name": "SystemInformation", "Value": "

System information

AMYL2: ACN 8570

SAMY2: ACN 8566 (STAT, reaction time: 7)

", "Language": "en" }, { "Name": "Handling", "Value": "

Reagent handling

Ready for use

", "Language": "en" }, { "Name": "TestDefinition", "Value": "

Application for serum, plasma and urine

cobas c 701/702 test definition

Assay type

Rate A

Reaction time / Assay points

10 / 31‑38 (STAT 7 / 19‑26)

Wavelength (sub/main)

700/415 nm

Reaction direction

Increase

Unit

U/L (µkat/L)

Reagent pipetting

Diluent (H2O)

R1

100 µL

R3 (STAT R2)

20 µL

Sample volumes

Sample

Sample dilution

Sample

Diluent (NaCl)

Normal

4 µL

Decreased

8 µL

15 µL

135 µL

Increased

8 µL

", "Language": "en" }, { "Name": "StorageStability", "Value": "

Storage and stability

AMYL2

Shelf life at 2‑8 °C:

See expiration date on cobas c pack label.

On‑board in use and refrigerated on the analyzer:

4 weeks

On‑board on the Reagent Manager:

24 hours

Diluent NaCl 9 %

Shelf life at 2‑8 °C:

See expiration date on cobas c pack label.

On‑board in use and refrigerated on the analyzer:

4 weeks

On‑board on the Reagent Manager:

24 hours

", "Language": "en" }, { "Name": "Calibration", "Value": "

Calibration

Calibrators

S1: H2O
S2: C.f.a.s.

Calibration mode

Linear

Calibration frequency

2‑point calibration
- after reagent lot change
- as required following quality control procedures

Calibration interval may be extended based on acceptable verification of calibration by the laboratory.

Traceability: This method has been standardized against Roche system reagent using calibrated pipettes together with a manual photometer providing absolute values and substrate-specific absorptivity, ε.

", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "

Specific performance data

Representative performance data on the analyzers are given below. Results obtained in individual laboratories may differ.

", "Language": "en" }, { "Name": "Precision", "Value": "

Precision

Precision was determined using human samples and controls in an internal protocol with repeatability (n = 21) and intermediate precision (3 aliquots per run, 1 run per day, 21 days). The following results were obtained:

Serum/plasma

AMYL2:

Repeatability

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Precinorm U

75.9 (1.27)

0.5 (0.01)

0.6

Precipath U

190 (3.17)

1 (0.02)

0.4

Human serum A

56.1 (0.937)

0.3 (0.005)

0.5

Human serum B

275 (4.59)

1 (0.02)

0.4

Human serum C

1273 (21.3)

5 (0.1)

0.4

SAMY2:

Repeatability

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Precinorm U

76.4 (1.28)

0.6 (0.00)

0.8

Precipath U

189 (3.16)

1 (0.02)

0.7

Human serum A

56.1 (0.937)

0.7 (0.012)

1.3

Human serum B

274 (4.58)

1 (0.02)

0.3

Human serum C

1265 (21.1)

6 (0.1)

0.5

AMYL2 / SAMY2:

Intermediate precision

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Precinorm U

84.0 (1.40)

1.1 (0.02)

1.3

Precipath U

184 (3.08)

3 (0.05)

1.5

Human serum 3

35.1 (0.586)

0.9 (0.015)

2.4

Human serum 4

98.9 (1.65)

1.6 (0.03)

1.6

Urine

AMYL2:

Repeatability

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Control level 1

48.9 (0.817)

0.4 (0.007)

0.9

Control level 2

147 (2.45)

1 (0.02)

0.5

Urine A

102 (1.70)

1 (0.02)

0.6

Urine B

527 (8.80)

2 (0.03)

0.4

Urine C

1401 (23.4)

5 (0.1)

0.3

SAMY2:

Repeatability

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Control level 1

48.8 (0.815)

0.4 (0.007)

0.9

Control level 2

146 (2.44)

1 (0.02)

0.5

Urine A

102 (1.70)

1 (0.02)

0.6

Urine B

523 (8.73)

2 (0.03)

0.4

Urine C

1395 (23.3)

8 (0.1)

0.6

AMYL2 / SAMY2:

Intermediate precision

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Control level 1

51.8 (0.865)

0.9 (0.015)

1.7

Control level 2

168 (2.81)

2 (0.03)

1.1

Urine 3

24.5 (0.409)

0.5 (0.008)

1.9

Urine 4

67.0 (1.12)

2.8 (0.05)

4.2

Results for intermediate precision were obtained on the master system cobas c 501 analyzer.

", "Language": "en" }, { "Name": "MethodComparison", "Value": "

Method comparison

Amylase values for human serum, plasma and urine samples obtained on a Roche/Hitachi cobas c 701 analyzer (y) were compared with those determined using the corresponding reagent on a Roche/Hitachi cobas c 501 analyzer (x).

Serum/plasma

Sample size (n) = 76

AMYL2:

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.022x - 0.467 U/L

y = 1.022x - 0.505 U/L

τ = 0.987

r = 1.000

The sample activities were between 21.0 and 1397 U/L (0.351 and 23.3 µkat/L).

SAMY2:

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.015x + 0.669 U/L

y = 1.014x + 1.83 U/L

τ = 0.984

r = 1.000

The sample activities were between 6.00 and 1403 U/L (0.100 and 23.4 µkat/L).

Urine

Sample size (n) = 82

AMYL2:

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.985x + 1.72 U/L

y = 0.970x + 5.21 U/L

τ = 0.987

r = 0.998

The sample activities were between 10.0 and 1296 U/L (0.167 and 21.6 µkat/L).

SAMY2:

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.989x + 1.18 U/L

y = 0.963x + 6.70 U/L

τ = 0.992

r = 0.998

The sample activities were between 11.0 and 1308 U/L (0.184 and 21.8 µkat/L).

", "Language": "en" }, { "Name": "Summary", "Value": "

Summary

Summary
LREFGreiling H, Gressner AM, eds. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3rd ed. Stuttgart/New York: Schattauer Verlag 1995.
,
LREFKeller H, ed. Klinisch-chemische Labordiagnostik für die Praxis, 2nd ed. Stuttgart/New York: Georg Thieme Verlag 1991:354-361.
,
LREFSalt WB II, Schenker S. Amylase - its clinical significance: a review of the literature [Review]. Medicine 1976;55:269-281.
,
LREFSteinberg WM, Goldstein SS, Davies ND, et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985;102:576-580.
,
LREFTietz NW, Huang WY, Rauh DF et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32:301-307.
,
LREFJunge W, Troge B, Klein G, et al. Evaluation of a New Assay for Pancreatic Amylase: Performance Characteristics and Estimation of Reference Intervals. Clin Biochem 1989;22:109-114.
,
LREFRauscher E, von Bülow S, Hägele EO et al.Fresenius Z Anal Chem 1986;324:304–5.
,
LREFKruse-Jarres JD, Hafkenscheid JCM, Hohenwallner W, et al. Evaluation of a New α-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-nitrophenyl-(G1)-α-D-maltoheptaoside as Substrate. J Clin Chem Clin Biochem 1989;27:103-113.
,
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC Clin Biochem/Erratum. Clin Biochem 2003;36:161.

The α‑amylases (1,4‑α‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4‑α‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ-specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.

Because of the sparsity of specific clinical symptoms of pancreatic diseases, α‑amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas-specific enzyme - lipase or pancreatic-α‑amylase - also be determined.

Numerous methods have been described for the determination of α‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme-catalyzed subsequent reactions. The kinetic method described here is based on the well-proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑α,D‑maltoheptaoside (Ethylidene Protected Substrate = EPS) by α‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC. This assay follows the recommendation of the IFCC, but was optimized for performance and stability.

", "Language": "en" }, { "Name": "Reagents", "Value": "

Reagents - working solutions

R1

HEPES: 52.4 mmol/L; sodium chloride: 87 mmol/L; calcium chloride: 0.08 mmol/L; magnesium chloride: 12.6 mmol/L; α‑glucosidase (microbial): ≥ 66.8 µkat/L; pH 7.0 (37 °C); preservatives; stabilizers

R3

(STAT R2)

HEPES: 52.4 mmol/L; ethylidene‑G7‑PNP: 22 mmol/L; pH 7.0 (37 °C); preservatives; stabilizers

R1 is in position B and R3 (STAT R2) is in position C.

", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "

Precautions and warnings

For in vitro diagnostic use for health care professionals. Exercise the normal precautions required for handling all laboratory reagents.

Infectious or microbial waste:
Warning: handle waste as potentially biohazardous material. Dispose of waste according to accepted laboratory instructions and procedures.

Environmental hazards:
Apply all relevant local disposal regulations to determine the safe disposal.

Safety data sheet available for professional user on request.

For USA: Caution: Federal law restricts this device to sale by or on the order of a physician.

This kit contains components classified as follows in accordance with the Regulation (EC) No. 1272/2008:

Warning

H317

May cause an allergic skin reaction.

Prevention:

P261

Avoid breathing dust/fume/gas/mist/vapours/spray.

P272

Contaminated work clothing should not be allowed out of the workplace.

P280

Wear protective gloves.

Response:

P333 + P313

If skin irritation or rash occurs: Get medical advice/attention.

P362 + P364

Take off contaminated clothing and wash it before reuse.

Disposal:

P501

Dispose of contents/container to an approved waste disposal plant.

Product safety labeling follows EU GHS guidance.

", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "

Quality control

For quality control, use control materials as listed in the “Order information” section. In addition, other suitable control material can be used.

The control intervals and limits should be adapted to each laboratory’s individual requirements. Values obtained should fall within the defined limits. Each laboratory should establish corrective measures to be taken if values fall outside the defined limits.

Follow the applicable government regulations and local guidelines for quality control.

", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "

Specimen collection and preparation

Specimen collection and preparation
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC Clin Biochem/Erratum. Clin Biochem 2003;36:161.
,
LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press, 1997, 2nd edition.

For specimen collection and preparation only use suitable tubes or collection containers.

Only the specimens listed below were tested and found acceptable.

Serum

Plasma: Li‑heparin plasma.

The sample types listed were tested with a selection of sample collection tubes that were commercially available at the time of testing, i.e. not all available tubes of all manufacturers were tested. Sample collection systems from various manufacturers may contain differing materials which could affect the test results in some cases. When processing samples in primary tubes (sample collection systems), follow the instructions of the tube manufacturer.

Centrifuge samples containing precipitates before performing the assay.

See the limitations and interferences section for details about possible sample interferences.

Sample stability claims were established by experimental data by the manufacturer or based on reference literature and only for the temperatures/time frames as stated in the method sheet. It is the responsibility of the individual laboratory to use all available references and/or its own studies to determine specific stability criteria for its laboratory.

Urine: Collect urine without additives. α‑Amylase is unstable in acid urine. Assay promptly or adjust pH to alkaline range (just above pH 7) before storage.

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

Stability in serum or plasma:

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

7 days at 15‑25 °C
1 month at 2‑8 °C

Stability in urine:

LREFHohenwallner W, Hägele EO, Scholer A, et al. Bestimmung von alpha-Amylase mit p-Nitrophenylmaltoheptaosid als Substrat. Ber Öster Ges Klin Chem 1983;6:101-112.

2 days at 15‑25 °C
10 days at 2‑8 °C

", "Language": "en" } ] } }, { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "05402603001", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "8", "DocumentObjectID": "FF0000000487890E", "DocumentOriginID": "FF000000002E600E", "MaterialNumbers": [ "05401496190" ], "InstrumentReferences": [ { "ID": "307", "BrandName": "cobas c 111" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "

Intended use

In vitro test for the quantitative determination of α‑amylase in human serum, plasma and urine on the cobas c 111 system.

", "Language": "en" }, { "Name": "TestPrinciple", "Value": "

Test principle

Test principle
LREFLorentz K. Approved recommendation on IFCC methods for the measurement of catalytic concentration of enzymes. Part 9. IFCC Method for α-Amylase. (1,4-α-D-Glucan 4-Glucanohydrolase, EC 3.2.1.1). Clin Chem Lab Med 1998;36(3):185-203.
,
LREFKurrle-Weitenhiller A, Hölzel W, Engel D, et al. Method for the determination of total and pancreatic α-amylase based on 100 % cleavage of the protected substrate ethylidene-4-nitrophenyl-maltoheptaoside. Clin Chem 1996;42(S6):98.

Enzymatic colorimetric assay acc. to IFCC

Defined oligosaccharides such as 4,6‑ethylidene-(G7)p‑nitrophenyl-(G1)-α,D‑maltoheptaoside (ethylidene-G7PNP) are cleaved under the catalytic action of α‑amylases. The G2PNP, G3PNP and G4PNP fragments so formed are completely hydrolyzed to p‑nitrophenol and glucose by α‑glucosidase.

Simplified reaction scheme:

α-amylase

5 ethylidene-G7PNP

FREFPNP = p-nitrophenol
+ 5 H2O

2 ethylidene-G5 + 2 G2PNP

+ 2 ethylidene-G4 + 2 G3PNP + ethylidene-G3 + G4PNP

α-glucosidase

2 G2PNP + 2 G3PNP + G4PNP + 14 H2O

  5 PNP + 14 G

FREFG = Glucose

The color intensity of the p-nitrophenol formed is directly proportional to the α‑amylase activity. It is determined by measuring the increase in absorbance.

", "Language": "en" }, { "Name": "MeasuringRange", "Value": "

Limits and ranges

Measuring range

Serum/plasma
3‑1500 U/L (0.05‑25.1 µkat/L)

Urine
3‑2000 U/L (0.05‑33.4 µkat/L)

Determine samples having higher activities via the rerun function. Dilution of samples via the rerun function is a 1:5 dilution. Results from samples diluted using the rerun function are automatically multiplied by a factor of 5.

Lower limits of measurement

Lower detection limit of the test:
3 U/L (0.05 µkat/L)

The lower detection limit represents the lowest measurable analyte level that can be distinguished from zero. It is calculated as the value lying 3 standard deviations above that of the lowest standard (standard 1 + 3 SD, repeatability, n = 21).

", "Language": "en" }, { "Name": "ExpectedValues", "Value": "

Expected values

Expected values
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC Clin Biochem/Erratum. Clin Biochem 2003;36:161.

Serum/plasma

Men/women

0.47-1.67 µkat/L

28-100 U/L

Spontaneously voided urine

Men

0.27-8.20 µkat/L

16-491 U/L

Women

0.35-7.46 µkat/L

21-447 U/L

α‑amylase/creatinine quotient

Men

0.97-4.73 µkat/g

58-283 U/g

Women

1.25-6.51 µkat/g

75-360 U/g

Each laboratory should investigate the transferability of the expected values to its own patient population and if necessary determine its own reference ranges.

α-Amylase/creatinine quotient

To allow for fluctuations in the α‑amylase activity in urine, it is advisable to determine the α‑amylase/creatinine quotient. To do this, determine the α‑amylase activity and creatinine concentration in spontaneously voided urine.

Quotient [µkat/mmol or U/g] =

 α‑amylase [µkat/L or U/L]
creatinine [mmol/L or g/L]

Amylase/Creatinine Clearance Ratio (ACCR)
LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

The ACCR is calculated from amylase activity and creatinine concentration. Both the serum and urine samples should be collected at the same time.

ACCR [%] =

urine amylase [U/L] × serum creatinine [mg/L]
serum amylase [U/L] × urine creatinine [mg/L]

× 100

ACCR is approximately equal to 2‑5 %

", "Language": "en" }, { "Name": "LimitationInterference", "Value": "

Limitations - interference

Limitations - interference
LREFYoung DS. Effects of Drugs on Clinical Laboratory Tests. 2nd edition, AACC Press 1997.

A slight change in the yellow coloration of solution 2 does not interfere with the performance of the test.

Do not pipette by mouth, and ensure that the reagent does not come into contact with the skin. Saliva and sweat contain α‑amylase!

Serum/plasma

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 100 U/L (1.67 µkat/L).

Icterus:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an I index of 52 for conjugated bilirubin and 60 for unconjugated bilirubin (approximate conjugated bilirubin concentration: 889 µmol/L or 52 mg/dL; approximate unconjugated bilirubin concentration: 1026 µmol/L or 60 mg/dL).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an H index of 260 (approximate hemoglobin concentration: 161 µmol/L or 260 mg/dL).

Lipemia (Intralipid):

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an L index of 2000. There is poor correlation between the L index (corresponds to turbidity) and triglycerides concentration.
Highly turbid and grossly lipemic samples may cause Abs. flags.

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFBreuer J. Report on the Symposium "Drug Effects in Clinical Chemistry Methods". Eur J Clin Chem Clin Biochem 1996;34:385-386.
,
LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Exception: Icodextrin-based drugs may lead to decreased amylase values.
LREFGokal R, Moberly J, Lindholm B, et al. Metabolic and laboratory effects of icodextrin. Kidney Int 2002;62(81):62-71.

Anticoagulants: Interference was found with citrate and fluoride.

In very rare cases, gammopathy, in particular type IgM (Waldenström’s macroglobulinemia), may cause unreliable results.

LREFBakker AJ, Mücke M. Gammopathy interference in clinical chemistry assays: mechanisms, detection and prevention. Clin Chem Lab Med 2007;45(9):1240-1243.

Urine

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 460 U/L (7.68 µkat/L).

Hemolysis: No significant interference up to a hemoglobin concentration of 311 µmol/L (500 mg/dL).

Phosphate: No significant interference from phosphate up to a concentration of 70 mmol/L (217 mg/dL).

Urea: No significant interference from urea up to a concentration of 1500 mmol/L (9009 mg/dL).

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

For diagnostic purposes, the results should always be assessed in conjunction with the patient’s medical history, clinical examination and other findings.

ACTION REQUIRED
Special Wash Programming: The use of special wash steps is mandatory when certain test combinations are run together on the cobas c 111 analyzer. For information about test combinations requiring special wash steps, please refer to the latest version of the carry-over evasion list found with the CLEAN Method Sheet and the operator’s manual for further instructions.
Where required, special wash/carry-over evasion programming must be implemented prior to reporting results with this test.

", "Language": "en" }, { "Name": "OrderInformation", "Value": "

OrderInformation_111 (CC Reagents - cobas + Integra)

Order information

Analyzer(s) on which kit(s) can be used

05401496 190

α-Amylase EPS ver.2 (2 × 100 tests)

cobasc 111

Materials required (but not provided):

10759350 190

Calibrator f.a.s. (12 × 3 mL)

Code 401

10759350 360

Calibrator f.a.s. (12 × 3 mL, for USA)

Code 401

12149435 122

Precinorm U plus (10 × 3 mL)

Code 300

12149435 160

Precinorm U plus (10 × 3 mL, for USA)

Code 300

12149443 122

Precipath U plus (10 × 3 mL)

Code 301

12149443 160

Precipath U plus (10 × 3 mL, for USA)

Code 301

05117003 190

PreciControl ClinChem Multi 1 (20 × 5 mL)

Code 391

05947626 190

PreciControl ClinChem Multi 1 (4 × 5 mL)

Code 391

05947626 160

PreciControl ClinChem Multi 1 (4 × 5 mL, for USA)

Code 391

05117216 190

PreciControl ClinChem Multi 2 (20 × 5 mL)

Code 392

05947774 190

PreciControl ClinChem Multi 2 (4 × 5 mL)

Code 392

05947774 160

PreciControl ClinChem Multi 2 (4 × 5 mL, for USA)

Code 392

", "Language": "en" }, { "Name": "SystemInformation", "Value": "

System information

AMYL2: ACN 570

AMYU2: ACN 301

", "Language": "en" }, { "Name": "Handling", "Value": "

Reagent handling

Ready for use

", "Language": "en" }, { "Name": "TestDefinition", "Value": "

Application for serum, plasma and urine

cobas c 111 test definition

Measuring mode

Absorbance

Abs. calculation mode

Kinetic

Reaction direction

Increase

Wavelength A/B

409/659 nm

Calc. first/last

26/38

Units

U/L (µkat/L)

Reaction mode

R1-S-SR

Pipetting parameters

Diluent (H2O)

R1

100 µL

Sample

4 µL

4 µL

SR

20 µL

Total volume

128 µL

", "Language": "en" }, { "Name": "StorageStability", "Value": "

Storage and stability

Shelf life at 2-8 °C:

See expiration date on reagent

On-board in use and refrigerated on the analyzer:

4 weeks

", "Language": "en" }, { "Name": "Calibration", "Value": "

Calibration

Calibrator

Calibrator f.a.s.

Deionized water is used automatically by the instrument as the zero calibrator.

Calibration mode

Linear regression

Calibration interval

Each lot and as required following quality control procedures

Calibration interval may be extended based on acceptable verification of calibration by the laboratory.

Traceability: This method has been standardized against Roche system reagent using calibrated pipettes together with a manual photometer providing absolute values and substrate-specific absorptivity, ε.

", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "

Specific performance data

Representative performance data on the cobas c 111 analyzer are given below. Results obtained in individual laboratories may differ.

", "Language": "en" }, { "Name": "Precision", "Value": "

Precision

Precision was determined using human samples and controls in an internal protocol with repeatability (n = 21) and intermediate precision (3 aliquots per run, 1 run per day, 10 days). The following results were obtained:

Serum/plasma

Repeatability

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Precinorm U

76.1 (1.27)

0.6 (0.01)

0.8

Precipath U

190 (3.17)

1 (0.02)

0.7

Human serum 1

57.9 (0.967)

0.7 (0.012)

1.1

Human serum 2

614 (10.3)

4 (0.1)

0.7

Intermediate precision

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Precinorm U

77.0 (1.29)

1.4 (0.02)

1.8

Precipath U

189 (3.16)

2 (0.03)

1.3

Human serum 1

57.2 (0.955)

1.4 (0.02)

2.5

Human serum 2

617 (10.3)

6 (0.1)

1.0

Urine

Repeatability

Mean
U/L (µkat/L)

SD
U/L (µkat/L)

CV
%

Control level 1

74.1 (1.24)

0.4 (0.01)

0.5

Control level 2

191 (3.2)

1 (0.02)

0.6

Urine sample 1

38.8 (0.648)

0.4 (0.007)

1.0

Urine sample 2

461 (7.70)

2 (0.03)

0.4

Urine sample 3

817 (13.6)

2 (0.03)

0.3

Urine sample 4

1699 (28.4)

9 (0.2)

0.6

", "Language": "en" }, { "Name": "MethodComparison", "Value": "

Method comparison

Amylase values for human samples obtained on the cobas c 111 analyzer (y) were compared with those determined using the same reagent on a COBAS INTEGRA 400 analyzer (x).

Serum/plasma

Sample size (n) = 85

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.01x – 0.60 U/L

y = 1.01x – 1.14 U/L

τ = 0.981

r = 1.000

The sample activities were between 12.9 and 1126 U/L (0.22 and 18.8 µkat/L).

Urine

Sample size (n) = 63

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.975x – 1.36 U/L

y = 0.973x – 1.08 U/L

τ = 0.988

r = 0.999

The sample activities were between 4.75 and 1966 U/L (0.08 and 32.8 µkat/L) on the reference system (x).

", "Language": "en" }, { "Name": "Summary", "Value": "

Summary

Summary
LREFGreiling H, Gressner AM, eds. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3rd ed. Stuttgart/New York: Schattauer Verlag 1995.
,
LREFKeller H, ed. Klinisch-chemische Labordiagnostik für die Praxis, 2nd ed. Stuttgart/New York: Georg Thieme Verlag 1991:354-361.
,
LREFSalt WB II, Schenker S. Amylase - its clinical significance: a review of the literature [Review]. Medicine 1976;55:269-281.
,
LREFSteinberg WM, Goldstein SS, Davies ND, et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985;102:576-580.
,
LREFTietz NW, Huang WY, Rauh DF, et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32(2):301-307.
,
LREFJunge W, Troge B, Klein G, et al. Evaluation of a New Assay for Pancreatic Amylase: Performance Characteristics and Estimation of Reference Intervals. Clin Biochem 1989;22:109-114.
,
LREFRauscher E, von Bülow S, Hägele EO, et al. Ethylidene protected substrate for the assay of human α-amylase. Fresenius Z Anal Chem 1986;324:304-305.
,
LREFKruse-Jarres JD, Hafkenscheid JCM, Hohenwallner W, et al. Evaluation of a New α-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-nitrophenyl-(G1)-α-D-maltoheptaoside as Substrate. J Clin Chem Clin Biochem 1989;27:103-113.
,
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC Clin Biochem/Erratum. Clin Biochem 2003;36:161.

The α‑amylases (1,4‑α-D-glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4-α-glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ-specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.

Because of the sparsity of specific clinical symptoms of pancreatic diseases, α‑amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas-specific enzyme - lipase or pancreatic-α-amylase - also be determined.

Numerous methods have been described for the determination of α‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme-catalyzed subsequent reactions. The kinetic method described here is based on the well-proven cleavage of 4,6-ethylidene-(G7)-1,4-nitrophenyl-(G1)-α,D-maltoheptaoside (Ethylidene Protected Substrate = EPS) by α‑amylase and subsequent hydrolysis of all the degradation products to p-nitrophenol with the aid of α‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC.

This assay follows the recommendation of the IFCC, but was optimized for performance and stability.

", "Language": "en" }, { "Name": "Reagents", "Value": "

Reagents - working solutions

R1

HEPES: 52.4 mmol/L; sodium chloride: 87 mmol/L; calcium chloride: 0.08 mmol/L; magnesium chloride: 12.6 mmol/L; α‑glucosidase (microbial): ≥ 66.8 µkat/L; pH 7.0 (37 °C); preservatives; stabilizers

SR

HEPES: 52.4 mmol/L; ethylidene-G7-PNP: 22 mmol/L; pH 7.0 (37 °C); preservatives; stabilizers

", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "

Precautions and warnings

For in vitro diagnostic use for health care professionals. Exercise the normal precautions required for handling all laboratory reagents.

Infectious or microbial waste:
Warning: handle waste as potentially biohazardous material. Dispose of waste according to accepted laboratory instructions and procedures.

Environmental hazards:
Apply all relevant local disposal regulations to determine the safe disposal.

Safety data sheet available for professional user on request.

For USA: Caution: Federal law restricts this device to sale by or on the order of a physician.

Warning

H317

May cause an allergic skin reaction.

Prevention:

P261

Avoid breathing dust/fume/gas/mist/vapours/spray.

P272

Contaminated work clothing should not be allowed out of the workplace.

P280

Wear protective gloves.

Response:

P333 + P313

If skin irritation or rash occurs: Get medical advice/attention.

P362 + P364

Take off contaminated clothing and wash it before reuse.

Disposal:

P501

Dispose of contents/container to an approved waste disposal plant.

Product safety labeling follows EU GHS guidance.

", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "

Quality control

Serum/plasma

For quality control, use control materials as listed in the “Order information” section. In addition, other suitable control material can be used.

Urine
Quantitative urine controls are recommended for routine quality control.

The control intervals and limits should be adapted to each laboratory’s individual requirements. Values obtained should fall within the defined limits. Each laboratory should establish corrective measures to be taken if values fall outside the defined limits.

Follow the applicable government regulations and local guidelines for quality control.

", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "

Specimen collection and preparation

Specimen collection and preparation
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC Clin Biochem/Erratum. Clin Biochem 2003;36:161.

For specimen collection and preparation only use suitable tubes or collection containers.

Only the specimens listed below were tested and found acceptable.
Serum
Plasma: Heparin (Li-, Na-, NH4+-) or EDTA (K2-, K3-) plasma.

EDTA plasma values are approximately 5‑10 % lower than serum values.

The sample types listed were tested with a selection of sample collection tubes that were commercially available at the time of testing, i.e. not all available tubes of all manufacturers were tested. Sample collection systems from various manufacturers may contain differing materials which could affect the test results in some cases. When processing samples in primary tubes (sample collection systems), follow the instructions of the tube manufacturer.

Urine
Collect urine without additives. α‑Amylase is unstable in acid urine. Assay promptly or adjust pH to alkaline range (just above pH 7) before storage.

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

See the limitations and interferences section for details about possible sample interferences.

Centrifuge samples containing precipitates before performing the assay.

Stability in serum or plasma:

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

7 days at 15‑25 °C

1 month at 2‑8 °C

Stability in urine:

LREFHohenwallner W, Hägele EO, Scholer A, et al. Bestimmung von alpha-Amylase mit p-Nitrophenylmaltoheptaosid als Substrat. Ber Öster Ges Klin Chem 1983;6:101-112.

2 days at 15‑25 °C

10 days at 2‑8 °C

Sample stability claims were established by experimental data by the manufacturer or based on reference literature and only for the temperatures/time frames as stated in the method sheet. It is the responsibility of the individual laboratory to use all available references and/or its own studies to determine specific stability criteria for its laboratory.

", "Language": "en" } ] } }, { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "0208056811190c503", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "3", "DocumentObjectID": "FF00000004CBCE0E", "DocumentOriginID": "FF00000004CBCD0E", "MaterialNumbers": [ "08056811190" ], "InstrumentReferences": [ { "ID": "9493", "BrandName": "cobas c 303" }, { "ID": "8481", "BrandName": "cobas c 503" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "

Intended use

In vitro test for the quantitative determination of α‑amylase in human serum, plasma and urine on Roche/Hitachi cobas c systems.

", "Language": "en" }, { "Name": "TestPrinciple", "Value": "

Test principle

Test principle
LREFLorentz K. Approved recommendation on IFCC methods for the measurement of catalytic concentration of enzymes. Part 9. IFCC Method for α-Amylase. (1,4-α-D-Glucan 4-Glucanohydrolase, EC 3.2.1.1). Clin Chem Lab Med 1998;36(3):185-203.
,
LREFKurrle-Weitenhiller A, Hölzel W, Engel D, et al. Method for the determination of total and pancreatic α-amylase based on 100 % cleavage of the protected substrate ethylidene-4-nitrophenyl-maltoheptaoside. Clin Chem 1996;42(S6):98.

Enzymatic colorimetric assay acc. to IFCC.

Defined oligosaccharides such as 4,6‑ethylidene‑(G7) p‑nitrophenyl‑(G1)‑α‑D‑maltoheptaoside (ethylidene‑G7PNP) are cleaved under the catalytic action of α‑amylases. The G2PNP, G3PNP and G4PNP fragments so formed are completely hydrolyzed to p‑nitrophenol and glucose by α‑glucosidase.

Simplified reaction scheme:

5 ethylidene‑G7PNP

FREFPNP p‑nitrophenol
 + 5 H2O

α-amylase

2 ethylidene‑G5 + 2 G2PNP + 2 ethylidene‑G4 + 2 G3PNP 
+ ethylidene‑G3 + G4PNP

2 G2PNP + 2 G3PNP + G4PNP + 14 H2O

α‑glucosidase

5 PNP + 14 G

FREFG Glucose

The color intensity of the p‑nitrophenol formed is directly proportional to the α‑amylase activity. It is determined by measuring the increase in absorbance.

", "Language": "en" }, { "Name": "MeasuringRange", "Value": "

Limits and ranges

Measuring range

Serum, plasma and urine

3‑1500 U/L (0.05‑25.0 µkat/L)

Determine samples having higher activities via the rerun function. Dilution of samples via the rerun function is a 1:5 dilution. Results from samples diluted using the rerun function are automatically multiplied by a factor of 5.

Lower limits of measurement

Limit of Blank, Limit of Detection and Limit of Quantitation

Limit of Blank

= 3 U/L (0.05 µkat/L)

Limit of Detection

= 3 U/L (0.05 µkat/L)

Limit of Quantitation

= 3 U/L (0.05 µkat/L)

The Limit of Blank, Limit of Detection and Limit of Quantitation were determined in accordance with the CLSI (Clinical and Laboratory Standards Institute) EP17‑A2 requirements.

The Limit of Blank is the 95th percentile value from n ≥ 60 measurements of analyte‑free samples over several independent series. The Limit of Blank corresponds to the activity below which analyte‑free samples are found with a probability of 95 %.

The Limit of Detection is determined based on the Limit of Blank and the standard deviation of low activity samples.

The Limit of Detection corresponds to the lowest analyte activity which can be detected (value above the Limit of Blank with a probability of 95 %).

The Limit of Quantitation is the lowest analyte activity that can be reproducibly measured with a total error of 20 %. It has been determined using low activity α‑amylase samples.

", "Language": "en" }, { "Name": "ExpectedValues", "Value": "

Expected values

Expected values
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

U/L

Serum/plasma

Men/Women

28‑100 U/L

Spontaneously voided urine

Men
Women

16‑491 U/L
21‑447 U/L

α‑amylase/
creatinine quotient

Men
Women

58‑283 U/g
75‑390 U/g

µkat/L*

Serum/plasma

Men/Women

0.47‑1.67 µkat/L

Spontaneously voided urine

Men
Women

0.27‑8.20 µkat/L
0.35‑7.46 µkat/L

α‑amylase/
creatinine quotient

Men
Women

0.97‑4.73 µkat/g
1.25‑6.51 µkat/g

*calculated by unit conversion factor

α‑Amylase/creatinine quotient

To allow for fluctuations in the α‑amylase activity in urine, it is advisable to determine the α‑amylase/creatinine quotient. To do this, determine the α‑amylase activity and creatinine concentration in spontaneously voided urine.

Quotient [µkat/mmol or U/g] =

α‑amylase [µkat/L or U/L]
creatinine [mmol/L or g/L]

Amylase/Creatinine Clearance Ratio (ACCR)
LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

The ACCR is calculated from amylase activity and creatinine concentration. Both the serum and urine samples should be collected at the same time.

ACCR [%] =

urine amylase [U/L] × serum creatinine [mg/L]
serum amylase [U/L] × urine creatinine [mg/L]

× 100

The ACCR is approximately equal to 2‑5 %.

Each laboratory should investigate the transferability of the expected values to its own patient population and if necessary determine its own reference ranges.

", "Language": "en" }, { "Name": "LimitationInterference", "Value": "

Limitations - interference

A slight change in the yellow coloration of solution 2 does not interfere with the performance of the test.

Do not pipette by mouth, and ensure that the reagent does not come into contact with the skin. Saliva and sweat contain α‑amylase!

Serum/plasma

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 100 U/L.

Icterus:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an I index of 60 for conjugated and unconjugated bilirubin (approximate conjugated and unconjugated bilirubin concentration: 1026 µmol/L or 60 mg/dL).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Lipemia (Intralipid):

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an L index of 1500. There is poor correlation between the L index (corresponds to turbidity) and triglycerides concentration.

In rare cases, samples with a combination of elevated turbidity (L‑index) and high Amylase activity may cause a >React or >Abs flag.

Highly turbid and grossly lipemic samples may cause Abs. flags.

Anticoagulants: Interference was found with citrate, fluoride, and EDTA.

LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

Glucose: No significant interference from glucose up to a concentration of 111 mmol/L (2000 mg/dL). Approximately 10 % higher recovery was found at glucose concentrations of 250 mmol/L (4500 mg/dL).

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 5.68 mmol/L (100 mg/dL).

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFBreuer J. Report on the Symposium "Drug effects in Clinical Chemistry Methods". Eur J Clin Chem Clin Biochem 1996;34:385-386.
,
LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Exception: Icodextrin‑based drugs may lead to decreased amylase results.
LREFGokal R, Moberly J, Lindholm B, et al. Metabolic and laboratory effects of icodextrin. Kidney Int 2002;62(81):62-71.

In very rare cases, gammopathy, in particular type IgM (Waldenström’s macroglobulinemia), may cause unreliable results.

LREFBakker AJ, Mücke M. Gammopathy interference in clinical chemistry assays: mechanisms, detection and prevention. Clin Chem Lab Med 2007;45(9):1240-1243.

Urine

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 460 U/L.

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 2.27 mmol/L (40 mg/dL). Approximately 15 % lower recovery was found at ascorbic acid concentrations of 22.7 mmol/L (400 mg/dL).

Hemolysis: No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Phosphate: No significant interference from phosphate up to a concentration of 70 mmol/L (217 mg/dL).

Urea: No significant interference from urea up to a concentration of 1500 mmol/L (9009 mg/dL).

For diagnostic purposes, the results should always be assessed in conjunction with the patient’s medical history, clinical examination and other findings.

ACTION REQUIRED
Special Wash Programming: The use of special wash steps is mandatory when certain test combinations are run together on cobas c systems. All special wash programming necessary for avoiding carry-over is available via the cobas link. The latest version of the carry-over evasion list can be found with the NaOHD/SMS/SCCS Method Sheet. For further instructions refer to the operator’s manual.

", "Language": "en" }, { "Name": "OrderInformation", "Value": "

OrderInformation (CC Reagents - cobas + Integra)

Order information

Analyzer(s) on which cobas c pack(s) can be used

08056811190

α‑Amylase EPS ver.2 (750 tests)

System‑ID 2017 001

cobas c 303, cobas c 503

10759350360

Calibrator f.a.s. (12 x 3 mL)

Code 20401

05947626160

PreciControl ClinChem Multi 1 (4 x 5 mL)

Code 20391

05947774160

PreciControl ClinChem Multi 2 (4 x 5 mL)

Code 20392

08063494190

Diluent NaCl 9 % (123 mL)

System‑ID 2906 001

", "Language": "en" }, { "Name": "SystemInformation", "Value": "

System information

AMYL2: ACN 20170 (Serum/plasma)

AMYL2U: ACN 20171 (Urine)

", "Language": "en" }, { "Name": "Handling", "Value": "

Reagent handling

Ready for use

", "Language": "en" }, { "Name": "TestDefinition", "Value": "

Application for serum, plasma and urine

Test definition

Reporting time

10 min

Wavelength (sub/main)

700/415 nm

Reagent pipetting

Diluent (H2O)

R1

78 µL

R3

16 µL

Sample volumes

Sample

Sample dilution

Sample

Diluent (NaCl)

Normal

3.1 µL

Decreased

3.1 µL

20 µL

80 µL

Increased

3.1 µL

For further information about the assay test definitions refer to the application parameters setting screen of the corresponding analyzer and assay.

", "Language": "en" }, { "Name": "StorageStability", "Value": "

Storage and stability

Shelf life at 2‑8 °C:

See expiration date on cobas c pack label.

On‑board in use and refrigerated on the analyzer:

26 weeks

", "Language": "en" }, { "Name": "Calibration", "Value": "

Calibration

Application for serum/plasma (ACN 20170)

Calibrators

S1: H2O

S2: C.f.a.s.

Calibration mode

Linear

Calibration frequency

Automatic full calibration
- after reagent lot change

Full calibration
- as required following quality control procedures

Application for urine (ACN 20171)
Transfer of calibration from serum/plasma application (ACN 20170)

Calibration interval may be extended based on acceptable verification of calibration by the laboratory.

Traceability: This method has been standardized against Roche system reagent using calibrated pipettes together with a manual photometer providing absolute values and substrate-specific absorptivity, ε.

", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "

Specific performance data

Representative performance data on the analyzers are given below. These data represent the performance of the analytical procedure itself.

Results obtained in individual laboratories may differ due to heterogenous sample materials, aging of analyzer components and mixture of reagents running on the analyzer.

", "Language": "en" }, { "Name": "Precision", "Value": "

Precision

Precision was determined using human samples and controls in accordance with the CLSI (Clinical and Laboratory Standards Institute) EP05‑A3 requirements with repeatability (n = 84) and intermediate precision (2 aliquots per run, 2 runs per day, 21 days). Results for repeatability and intermediate precision were obtained on the cobas c 503 analyzer.

Serum/plasma

Repeatability

Mean
U/L

SD
U/L

CV
%

PCCC1c)

76.9

0.438

0.6

PCCC2d)

193

0.831

0.4

Human serum 1

7.38

0.231

3.1

Human serum 2

63.9

0.345

0.5

Human serum 3

509

1.63

0.3

Human serum 4

771

2.67

0.3

Human serum 5

1395

4.13

0.3

Intermediate precision

Mean
U/L

SD
U/L

CV
%

PCCC1

FREFPreciControl ClinChem Multi 1

76.9

0.713

0.9

PCCC2

FREFPreciControl ClinChem Multi 2

194

1.51

0.8

Human serum 1

7.38

0.263

3.6

Human serum 2

63.6

0.409

0.6

Human serum 3

509

2.51

0.5

Human serum 4

771

4.13

0.5

Human serum 5

1395

6.04

0.4

Urine

Repeatability

Mean
U/L

SD
U/L

CV
%

Control 1e)

56.3

0.327

0.6

Control 2e)

180

0.707

0.4

Human urine 1

7.78

0.257

3.3

Human urine 2

263

0.913

0.3

Human urine 3

408

1.13

0.3

Human urine 4

766

1.96

0.3

Human urine 5

1385

3.62

0.3

Intermediate precision

Mean
U/L

SD
U/L

CV
%

Control 1

FREFcommercially available control material

56.3

0.370

0.7

Control 2

FREFcommercially available control material

180

0.801

0.4

Human urine 1

7.74

0.403

5.2

Human urine 2

263

2.09

0.8

Human urine 3

409

10.6

2.6

Human urine 4

767

4.41

0.6

Human urine 5

1385

5.66

0.4

", "Language": "en" }, { "Name": "MethodComparison", "Value": "

Method comparison

Amylase values for human serum, plasma and urine samples obtained on acobas c 503 analyzer (y) were compared to those determined using the corresponding reagent on a cobas c 501 analyzer (x).

Serum/plasma

Sample size (n) = 85

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.006x − 0.00259 U/L

y = 1.008x − 0.399 U/L

τ = 0.993

r = 1.000

The sample activities were between 10.3 and 1439 U/L.

Urine

Sample size (n) = 67

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.997x + 0.221 U/L

y = 0.996x + 0.571 U/L

τ = 0.985

r = 1.000

The sample activities were between 6.90 and 1467 U/L.

Amylase values for human serum, plasma and urine samples obtained on a cobas c 303 analyzer (y) were compared to those determined using the corresponding reagent on a cobas c 501 analyzer (x).

Serum/plasma

Sample size (n) = 73

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.013x − 0.271 U/L

y = 1.012x − 0.182 U/L

τ = 0.993

r = 1.000

The sample activities were between 9.10 and 1460 U/L.

Urine

Sample size (n) = 71

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.014x - 0.186 U/L

y = 1.019x - 0.515 U/L

τ = 0.991

r = 1.000

The sample activities were between 4.80 and 1444 U/L.

", "Language": "en" }, { "Name": "Summary", "Value": "

Summary

Summary
LREFGreiling H, Gressner AM, eds. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3rd ed. Stuttgart/New York: Schattauer Verlag 1995.
,
LREFKeller H, ed. Klinisch-chemische Labordiagnostik für die Praxis, 2nd ed. Stuttgart/New York: Georg Thieme Verlag 1991:354-361.
,
LREFSalt WB II, Schenker S. Amylase - its clinical significance: a review of the literature [Review]. Medicine 1976;55:269-281.
,
LREFSteinberg WM, Goldstein SS, Davies ND, et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985;102:576-580.
,
LREFTietz NW, Huang WY, Rauh DF, et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32(2):301-307.
,
LREFJunge W, Troge B, Klein G, et al. Evaluation of a New Assay for Pancreatic Amylase: Performance Characteristics and Estimation of Reference Intervals. Clin Biochem 1989;22:109-114.
,
LREFRauscher E, von Bülow S, Hägele EO, et al. Ethylidene protected substrate for the assay of human α-amylase. Fresenius Z Anal Chem 1986;324:304-305.
,
LREFKruse-Jarres JD, Hafkenscheid JCM, Hohenwallner W, et al. Evaluation of a New α-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-nitrophenyl-(G1)-α-D-maltoheptaoside as Substrate. J Clin Chem Clin Biochem 1989;27:103-113.
,
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

The α‑amylases (1,4‑α‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4‑α‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ‑specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.

Because of the sparsity of specific clinical symptoms of pancreatic diseases, α‑amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas‑specific enzyme ‑ lipase or pancreatic‑α‑amylase ‑ also be determined.

Numerous methods have been described for the determination of α‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme‑catalyzed subsequent reactions. The kinetic method described here is based on the well‑proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑α,D‑maltoheptaoside (Ethylidene Protected Substrate = EPS) by α‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC. This assay follows the recommendation of the IFCC, but was optimized for performance and stability.

", "Language": "en" }, { "Name": "Reagents", "Value": "

Reagents - working solutions

R1

HEPES: 52.4 mmol/L; sodium chloride: 87 mmol/L; calcium chloride: 0.08 mmol/L; magnesium chloride: 12.6 mmol/L; α‑glucosidase (microbial): ≥ 66.8 µkat/L; pH 7.0 (37 °C); preservatives; stabilizers

R3

HEPES: 52.4 mmol/L; ethylidene‑G7‑PNP: 22 mmol/L; pH 7.0 (37 °C); preservatives; stabilizers

R1 is in position B and R3 is in position C.

", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "

Precautions and warnings

For in vitro diagnostic use.
Exercise the normal precautions required for handling all laboratory reagents.
Disposal of all waste material should be in accordance with local guidelines.
Safety data sheet available for professional user on request.

For USA: Caution: Federal law restricts this device to sale by or on the order of a physician.

This kit contains components classified as follows in accordance with the Regulation (EC) No. 1272/2008:

Warning

H317

May cause an allergic skin reaction.

Prevention:

P261

Avoid breathing dust/fume/gas/mist/vapours/spray.

P272

Contaminated work clothing should not be allowed out of the workplace.

P280

Wear protective gloves.

Response:

P333 + P313

If skin irritation or rash occurs: Get medical advice/attention.

P362 + P364

Take off contaminated clothing and wash it before reuse.

Disposal:

P501

Dispose of contents/container to an approved waste disposal plant.

Product safety labeling follows EU GHS guidance.

Contact phone: 1-800-428-2336

", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "

Quality control

For quality control, use control materials as listed in the \"Order information\" section.

In addition, other suitable control material can be used.

Serum/plasma:

PreciControl ClinChem Multi 1
PreciControl ClinChem Multi 2

Urine:

Quantitative urine controls are recommended for routine quality control.

The control intervals and limits should be adapted to each laboratory’s individual requirements. It is recommended to perform quality control always after lot calibration and subsequently at least every 26 weeks. Values obtained should fall within the defined limits. Each laboratory should establish corrective measures to be taken if values fall outside the defined limits.

Follow the applicable government regulations and local guidelines for quality control.

", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "

Specimen collection and preparation

Specimen collection and preparation
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.
,
LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

For specimen collection and preparation only use suitable tubes or collection containers.

Only the specimens listed below were tested and found acceptable.
Serum
Plasma: Li‑heparin plasma

The sample types listed were tested with a selection of sample collection tubes that were commercially available at the time of testing, i.e. not all available tubes of all manufacturers were tested. Sample collection systems from various manufacturers may contain differing materials which could affect the test results in some cases. When processing samples in primary tubes (sample collection systems), follow the instructions of the tube manufacturer.

Centrifuge samples containing precipitates before performing the assay.

Urine: Collect urine without additives. α‑Amylase is unstable in acid urine. Assay promptly or adjust pH to alkaline range (just above pH 7) before storage.

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

If stabilizers are added to the sample, the sample index feature must not be used.

See the limitations and interferences section for details about possible sample interferences.

Stability in serum or plasma:

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

7 days at 15‑25 °C

1 month at 2‑8 °C

Stability in urine:

LREFHohenwallner W, Hägele EO, Scholer A, et al. Bestimmung von alpha-Amylase mit p-Nitrophenylmaltoheptaosid als Substrat. Ber Öster Ges Klin Chem 1983;6:101-112.

2 days at 15‑25 °C

10 days at 2‑8 °C

Sample stability claims were established by experimental data by the manufacturer or based on reference literature and only for the temperatures/time frames as stated in the method sheet. It is the responsibility of the individual laboratory to use all available references and/or its own studies to determine specific stability criteria for its laboratory.

", "Language": "en" } ] } }, { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "0008056811190c503", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "4", "DocumentObjectID": "FF00000004876C0E", "DocumentOriginID": "FF000000028D750E", "MaterialNumbers": [ "08056811190" ], "InstrumentReferences": [ { "ID": "8481", "BrandName": "cobas c 503" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "

Intended use

In vitro test for the quantitative determination of α‑amylase in human serum, plasma and urine on Roche/Hitachi cobas c systems.

", "Language": "en" }, { "Name": "TestPrinciple", "Value": "

Test principle

Test principle
LREFLorentz K. Approved recommendation on IFCC methods for the measurement of catalytic concentration of enzymes. Part 9. IFCC Method for α-Amylase. (1,4-α-D-Glucan 4-Glucanohydrolase, EC 3.2.1.1). Clin Chem Lab Med 1998;36(3):185-203.
,
LREFKurrle-Weitenhiller A, Hölzel W, Engel D, et al. Method for the determination of total and pancreatic α-amylase based on 100 % cleavage of the protected substrate ethylidene-4-nitrophenyl-maltoheptaoside. Clin Chem 1996;42(S6):98.

Enzymatic colorimetric assay acc. to IFCC.

Defined oligosaccharides such as 4,6‑ethylidene‑(G7) p‑nitrophenyl‑(G1)‑α‑D‑maltoheptaoside (ethylidene‑G7PNP) are cleaved under the catalytic action of α‑amylases. The G2PNP, G3PNP and G4PNP fragments so formed are completely hydrolyzed to p‑nitrophenol and glucose by α‑glucosidase.

Simplified reaction scheme:

5 ethylidene‑G7PNP

FREFPNP p‑nitrophenol
 + 5 H2O

α-amylase

2 ethylidene‑G5 + 2 G2PNP + 2 ethylidene‑G4 + 2 G3PNP 
+ ethylidene‑G3 + G4PNP

2 G2PNP + 2 G3PNP + G4PNP + 14 H2O

α‑glucosidase

5 PNP + 14 G

FREFG Glucose

The color intensity of the p‑nitrophenol formed is directly proportional to the α‑amylase activity. It is determined by measuring the increase in absorbance.

", "Language": "en" }, { "Name": "MeasuringRange", "Value": "

Limits and ranges

Measuring range

Serum, plasma and urine

3‑1500 U/L (0.05‑25.0 µkat/L)

Determine samples having higher activities via the rerun function. Dilution of samples via the rerun function is a 1:5 dilution. Results from samples diluted using the rerun function are automatically multiplied by a factor of 5.

Lower limits of measurement

Limit of Blank, Limit of Detection and Limit of Quantitation

Limit of Blank

= 3 U/L (0.05 µkat/L)

Limit of Detection

= 3 U/L (0.05 µkat/L)

Limit of Quantitation

= 3 U/L (0.05 µkat/L)

The Limit of Blank, Limit of Detection and Limit of Quantitation were determined in accordance with the CLSI (Clinical and Laboratory Standards Institute) EP17‑A2 requirements.

The Limit of Blank is the 95th percentile value from n ≥ 60 measurements of analyte‑free samples over several independent series. The Limit of Blank corresponds to the activity below which analyte‑free samples are found with a probability of 95 %.

The Limit of Detection is determined based on the Limit of Blank and the standard deviation of low activity samples.

The Limit of Detection corresponds to the lowest analyte activity which can be detected (value above the Limit of Blank with a probability of 95 %).

The Limit of Quantitation is the lowest analyte activity that can be reproducibly measured with a total error of 20 %. It has been determined using low activity α‑amylase samples.

", "Language": "en" }, { "Name": "ExpectedValues", "Value": "

Expected values

Expected values
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

U/L

Serum/plasma

Men/Women

28‑100 U/L

Spontaneously voided urine

Men
Women

16‑491 U/L
21‑447 U/L

α‑amylase/
creatinine quotient

Men
Women

58‑283 U/g
75‑390 U/g

µkat/L*

Serum/plasma

Men/Women

0.47‑1.67 µkat/L

Spontaneously voided urine

Men
Women

0.27‑8.20 µkat/L
0.35‑7.46 µkat/L

α‑amylase/
creatinine quotient

Men
Women

0.97‑4.73 µkat/g
1.25‑6.51 µkat/g

*calculated by unit conversion factor

α‑Amylase/creatinine quotient

To allow for fluctuations in the α‑amylase activity in urine, it is advisable to determine the α‑amylase/creatinine quotient. To do this, determine the α‑amylase activity and creatinine concentration in spontaneously voided urine.

Quotient [µkat/mmol or U/g] =

α‑amylase [µkat/L or U/L]
creatinine [mmol/L or g/L]

Amylase/Creatinine Clearance Ratio (ACCR)
LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

The ACCR is calculated from amylase activity and creatinine concentration. Both the serum and urine samples should be collected at the same time.

ACCR [%] =

urine amylase [U/L] × serum creatinine [mg/L]
serum amylase [U/L] × urine creatinine [mg/L]

× 100

The ACCR is approximately equal to 2‑5 %.

Each laboratory should investigate the transferability of the expected values to its own patient population and if necessary determine its own reference ranges.

", "Language": "en" }, { "Name": "LimitationInterference", "Value": "

Limitations - interference

A slight change in the yellow coloration of solution 2 does not interfere with the performance of the test.

Do not pipette by mouth, and ensure that the reagent does not come into contact with the skin. Saliva and sweat contain α‑amylase!

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 100 U/L.

Serum/plasma

Icterus:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an I index of 60 for conjugated and unconjugated bilirubin (approximate conjugated and unconjugated bilirubin concentration: 1026 µmol/L or 60 mg/dL).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Lipemia (Intralipid):

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an L index of 1500. There is poor correlation between the L index (corresponds to turbidity) and triglycerides concentration.

In rare cases, samples with a combination of elevated turbidity (L‑index) and high Amylase activity may cause a >React or >Abs flag.

Highly turbid and grossly lipemic samples may cause Abs. flags.

Anticoagulants: Interference was found with citrate, fluoride, and EDTA.

LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

Glucose: No significant interference from glucose up to a concentration of 111 mmol/L (2000 mg/dL). Approximately 10 % higher recovery was found at glucose concentrations of 250 mmol/L (4500 mg/dL).

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 5.68 mmol/L (100 mg/dL).

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFBreuer J. Report on the Symposium "Drug effects in Clinical Chemistry Methods". Eur J Clin Chem Clin Biochem 1996;34:385-386.
,
LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Exception: Icodextrin‑based drugs may lead to decreased amylase results.
LREFGokal R, Moberly J, Lindholm B, et al. Metabolic and laboratory effects of icodextrin. Kidney Int 2002;62(81):62-71.

In very rare cases, gammopathy, in particular type IgM (Waldenström’s macroglobulinemia), may cause unreliable results.

LREFBakker AJ, Mücke M. Gammopathy interference in clinical chemistry assays: mechanisms, detection and prevention. Clin Chem Lab Med 2007;45(9):1240-1243.

Urine

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 2.27 mmol/L (40 mg/dL). Approximately 15 % lower recovery was found at ascorbic acid concentrations of 22.7 mmol/L (400 mg/dL).

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 460 U/L.

Hemolysis: No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Phosphate: No significant interference from phosphate up to a concentration of 70 mmol/L (217 mg/dL).

Urea: No significant interference from urea up to a concentration of 1500 mmol/L (9009 mg/dL).

For diagnostic purposes, the results should always be assessed in conjunction with the patient’s medical history, clinical examination and other findings.

ACTION REQUIRED
Special Wash Programming: The use of special wash steps is mandatory when certain test combinations are run together on Roche/Hitachi cobas c systems. All special wash programming necessary for avoiding carry-over is available via the cobas link. The latest version of the carry-over evasion list can be found with the NaOHD/SMS/SCCS Method Sheet for information. For further instructions refer to the operator’s manual.

", "Language": "en" }, { "Name": "OrderInformation", "Value": "

OrderInformation (CC Reagents - cobas + Integra)

Order information

Analyzer(s) on which cobas c pack(s) can be used

08056811 190

α‑Amylase EPS ver.2 (750 tests)

System‑ID 2017 001

Roche/Hitachi cobas c 503

Materials required (but not provided):

10759350 190

Calibrator f.a.s. (12 x 3 mL)

Code 20401

10759350 360

Calibrator f.a.s. (12 x 3 mL, for USA)

Code 20401

05117003 190

PreciControl ClinChem Multi 1 (20 x 5 mL)

Code 20391

05947626 190

PreciControl ClinChem Multi 1 (4 x 5 mL)

Code 20391

05947626 160

PreciControl ClinChem Multi 1 (4 x 5 mL, for USA)

Code 20391

05117216 190

PreciControl ClinChem Multi 2 (20 x 5 mL)

Code 20392

05947774 190

PreciControl ClinChem Multi 2 (4 x 5 mL)

Code 20392

05947774 160

PreciControl ClinChem Multi 2 (4 x 5 mL, for USA)

Code 20392

08063494 190

Diluent NaCl 9 % (123 mL)

System‑ID 2906 001

", "Language": "en" }, { "Name": "SystemInformation", "Value": "

System information

AMYL2: ACN 20170 (Serum/plasma)

AMYL2U: ACN 20171 (Urine)

", "Language": "en" }, { "Name": "Handling", "Value": "

Reagent handling

Ready for use

", "Language": "en" }, { "Name": "TestDefinition", "Value": "

Application for serum, plasma and urine

Test definition

Reporting time

10 min

Wavelength (sub/main)

700/415 nm

Reagent pipetting

Diluent (H2O)

R1

78 µL

R3

16 µL

Sample volumes

Sample

Sample dilution

Sample

Diluent (NaCl)

Normal

3.1 µL

Decreased

3.1 µL

20 µL

80 µL

Increased

3.1 µL

For further information about the assay test definitions refer to the application parameters setting screen of the corresponding analyzer and assay.

", "Language": "en" }, { "Name": "StorageStability", "Value": "

Storage and stability

Shelf life at 2‑8 °C:

See expiration date on cobas c pack label.

On‑board in use and refrigerated on the analyzer:

26 weeks

", "Language": "en" }, { "Name": "Calibration", "Value": "

Calibration

Application for serum/plasma (ACN 20170)

Calibrators

S1: H2O

S2: C.f.a.s.

Calibration mode

Linear

Calibration frequency

Automatic full calibration
- after reagent lot change

Full calibration
- as required following quality control procedures

Application for urine (ACN 20171)
Transfer of calibration from serum/plasma application (ACN 20170)

Calibration interval may be extended based on acceptable verification of calibration by the laboratory.

Traceability: This method has been standardized against Roche system reagent using calibrated pipettes together with a manual photometer providing absolute values and substrate-specific absorptivity, ε.

", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "

Specific performance data

Representative performance data on the analyzers are given below. These data represent the performance of the analytical procedure itself.

Results obtained in individual laboratories may differ due to heterogenous sample materials, aging of analyzer components and mixture of reagents running on the analyzer.

", "Language": "en" }, { "Name": "Precision", "Value": "

Precision

Precision was determined using human samples and controls in accordance with the CLSI (Clinical and Laboratory Standards Institute) EP05‑A3 requirements with repeatability (n = 84) and intermediate precision (2 aliquots per run, 2 runs per day, 21 days). The following results were obtained:

Serum/plasma

Repeatability

Mean
U/L

SD
U/L

CV
%

PCCC1c)

76.9

0.438

0.6

PCCC2d)

193

0.831

0.4

Human serum 1

7.38

0.231

3.1

Human serum 2

63.9

0.345

0.5

Human serum 3

509

1.63

0.3

Human serum 4

771

2.67

0.3

Human serum 5

1395

4.13

0.3

Intermediate precision

Mean
U/L

SD
U/L

CV
%

PCCC1

FREFPreciControl ClinChem Multi 1

76.9

0.713

0.9

PCCC2

FREFPreciControl ClinChem Multi 2

194

1.51

0.8

Human serum 1

7.38

0.263

3.6

Human serum 2

63.6

0.409

0.6

Human serum 3

509

2.51

0.5

Human serum 4

771

4.13

0.5

Human serum 5

1395

6.04

0.4

Urine

Repeatability

Mean
U/L

SD
U/L

CV
%

Control 1e)

56.3

0.327

0.6

Control 2e)

180

0.707

0.4

Human urine 1

7.78

0.257

3.3

Human urine 2

263

0.913

0.3

Human urine 3

408

1.13

0.3

Human urine 4

766

1.96

0.3

Human urine 5

1385

3.62

0.3

Intermediate precision

Mean
U/L

SD
U/L

CV
%

Control 1

FREFcommercially available control material

56.3

0.370

0.7

Control 2

FREFcommercially available control material

180

0.801

0.4

Human urine 1

7.74

0.403

5.2

Human urine 2

263

2.09

0.8

Human urine 3

409

10.6

2.6

Human urine 4

767

4.41

0.6

Human urine 5

1385

5.66

0.4

", "Language": "en" }, { "Name": "MethodComparison", "Value": "

Method comparison

Amylase values for human serum, plasma and urine samples obtained on a Roche/Hitachi cobas c 503 analyzer (y) were compared to those determined using the corresponding reagent on a Roche/Hitachi cobas c 501 analyzer (x).

Serum/plasma

Sample size (n) = 85

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.006x − 0.00259 U/L

y = 1.008x − 0.399 U/L

τ = 0.993

r = 1.000

The sample activities were between 10.3 and 1439 U/L.

Urine

Sample size (n) = 67

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.997x + 0.221 U/L

y = 0.996x + 0.571 U/L

τ = 0.985

r = 1.000

The sample activities were between 6.90 and 1467 U/L.

", "Language": "en" }, { "Name": "Summary", "Value": "

Summary

Summary
LREFGreiling H, Gressner AM, eds. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3rd ed. Stuttgart/New York: Schattauer Verlag 1995.
,
LREFKeller H, ed. Klinisch-chemische Labordiagnostik für die Praxis, 2nd ed. Stuttgart/New York: Georg Thieme Verlag 1991:354-361.
,
LREFSalt WB II, Schenker S. Amylase - its clinical significance: a review of the literature [Review]. Medicine 1976;55:269-281.
,
LREFSteinberg WM, Goldstein SS, Davies ND, et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985;102:576-580.
,
LREFTietz NW, Huang WY, Rauh DF, et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32(2):301-307.
,
LREFJunge W, Troge B, Klein G, et al. Evaluation of a New Assay for Pancreatic Amylase: Performance Characteristics and Estimation of Reference Intervals. Clin Biochem 1989;22:109-114.
,
LREFRauscher E, von Bülow S, Hägele EO, et al. Ethylidene protected substrate for the assay of human α-amylase. Fresenius Z Anal Chem 1986;324:304-305.
,
LREFKruse-Jarres JD, Hafkenscheid JCM, Hohenwallner W, et al. Evaluation of a New α-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-nitrophenyl-(G1)-α-D-maltoheptaoside as Substrate. J Clin Chem Clin Biochem 1989;27:103-113.
,
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

The α‑amylases (1,4‑α‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4‑α‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ‑specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.

Because of the sparsity of specific clinical symptoms of pancreatic diseases, α‑amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas‑specific enzyme ‑ lipase or pancreatic‑α‑amylase ‑ also be determined.

Numerous methods have been described for the determination of α‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme‑catalyzed subsequent reactions. The kinetic method described here is based on the well‑proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑α,D‑maltoheptaoside (Ethylidene Protected Substrate = EPS) by α‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC. This assay follows the recommendation of the IFCC, but was optimized for performance and stability.

", "Language": "en" }, { "Name": "Reagents", "Value": "

Reagents - working solutions

R1

HEPES: 52.4 mmol/L; sodium chloride: 87 mmol/L; calcium chloride: 0.08 mmol/L; magnesium chloride: 12.6 mmol/L; α‑glucosidase (microbial): ≥ 66.8 µkat/L; pH 7.0 (37 °C); preservatives; stabilizers

R3

HEPES: 52.4 mmol/L; ethylidene‑G7‑PNP: 22 mmol/L; pH 7.0 (37 °C); preservatives; stabilizers

R1 is in position B and R3 is in position C.

", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "

Precautions and warnings

For in vitro diagnostic use for health care professionals. Exercise the normal precautions required for handling all laboratory reagents.

Infectious or microbial waste:
Warning: handle waste as potentially biohazardous material. Dispose of waste according to accepted laboratory instructions and procedures.

Environmental hazards:
Apply all relevant local disposal regulations to determine the safe disposal.

Safety data sheet available for professional user on request.

For USA: Caution: Federal law restricts this device to sale by or on the order of a physician.

This kit contains components classified as follows in accordance with the Regulation (EC) No. 1272/2008:

Warning

H317

May cause an allergic skin reaction.

Prevention:

P261

Avoid breathing dust/fume/gas/mist/vapours/spray.

P272

Contaminated work clothing should not be allowed out of the workplace.

P280

Wear protective gloves.

Response:

P333 + P313

If skin irritation or rash occurs: Get medical advice/attention.

P362 + P364

Take off contaminated clothing and wash it before reuse.

Disposal:

P501

Dispose of contents/container to an approved waste disposal plant.

Product safety labeling follows EU GHS guidance.

", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "

Quality control

For quality control, use control materials as listed in the “Order information” section. In addition, other suitable control material can be used.

Serum/plasma:

PreciControl ClinChem Multi 1
PreciControl ClinChem Multi 2

Urine:

Quantitative urine controls are recommended for routine quality control.

The control intervals and limits should be adapted to each laboratory’s individual requirements. It is recommended to perform quality control always after lot calibration and subsequently at least every 26 weeks. Values obtained should fall within the defined limits. Each laboratory should establish corrective measures to be taken if values fall outside the defined limits.

Follow the applicable government regulations and local guidelines for quality control.

", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "

Specimen collection and preparation

Specimen collection and preparation
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.
,
LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

For specimen collection and preparation only use suitable tubes or collection containers.

Only the specimens listed below were tested and found acceptable.
Serum
Plasma: Li‑heparin plasma

The sample types listed were tested with a selection of sample collection tubes that were commercially available at the time of testing, i.e. not all available tubes of all manufacturers were tested. Sample collection systems from various manufacturers may contain differing materials which could affect the test results in some cases. When processing samples in primary tubes (sample collection systems), follow the instructions of the tube manufacturer.

Centrifuge samples containing precipitates before performing the assay.

Urine: Collect urine without additives. α‑Amylase is unstable in acid urine. Assay promptly or adjust pH to alkaline range (just above pH 7) before storage.

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

If stabilizers are added to the sample, the sample index feature must not be used.

See the limitations and interferences section for details about possible sample interferences.

Stability in serum or plasma:

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

7 days at 15‑25 °C

1 month at 2‑8 °C

Stability in urine:

LREFHohenwallner W, Hägele EO, Scholer A, et al. Bestimmung von alpha-Amylase mit p-Nitrophenylmaltoheptaosid als Substrat. Ber Öster Ges Klin Chem 1983;6:101-112.

2 days at 15‑25 °C

10 days at 2‑8 °C

Sample stability claims were established by experimental data by the manufacturer or based on reference literature and only for the temperatures/time frames as stated in the method sheet. It is the responsibility of the individual laboratory to use all available references and/or its own studies to determine specific stability criteria for its laboratory.

", "Language": "en" } ] } }, { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "0108056811190c503", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "5", "DocumentObjectID": "FF000000049CC90E", "DocumentOriginID": "FF000000045B060E", "MaterialNumbers": [ "08056811190" ], "InstrumentReferences": [ { "ID": "9493", "BrandName": "cobas c 303" }, { "ID": "8481", "BrandName": "cobas c 503" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "

Intended use

In vitro test for the quantitative determination of α‑amylase in human serum, plasma and urine on Roche/Hitachi cobas c systems.

", "Language": "en" }, { "Name": "TestPrinciple", "Value": "

Test principle

Test principle
LREFLorentz K. Approved recommendation on IFCC methods for the measurement of catalytic concentration of enzymes. Part 9. IFCC Method for α-Amylase. (1,4-α-D-Glucan 4-Glucanohydrolase, EC 3.2.1.1). Clin Chem Lab Med 1998;36(3):185-203.
,
LREFKurrle-Weitenhiller A, Hölzel W, Engel D, et al. Method for the determination of total and pancreatic α-amylase based on 100 % cleavage of the protected substrate ethylidene-4-nitrophenyl-maltoheptaoside. Clin Chem 1996;42(S6):98.

Enzymatic colorimetric assay acc. to IFCC.

Defined oligosaccharides such as 4,6‑ethylidene‑(G7) p‑nitrophenyl‑(G1)‑α‑D‑maltoheptaoside (ethylidene‑G7PNP) are cleaved under the catalytic action of α‑amylases. The G2PNP, G3PNP and G4PNP fragments so formed are completely hydrolyzed to p‑nitrophenol and glucose by α‑glucosidase.

Simplified reaction scheme:

5 ethylidene‑G7PNP

FREFPNP p‑nitrophenol
 + 5 H2O

α-amylase

2 ethylidene‑G5 + 2 G2PNP + 2 ethylidene‑G4 + 2 G3PNP 
+ ethylidene‑G3 + G4PNP

2 G2PNP + 2 G3PNP + G4PNP + 14 H2O

α‑glucosidase

5 PNP + 14 G

FREFG Glucose

The color intensity of the p‑nitrophenol formed is directly proportional to the α‑amylase activity. It is determined by measuring the increase in absorbance.

", "Language": "en" }, { "Name": "MeasuringRange", "Value": "

Limits and ranges

Measuring range

Serum, plasma and urine

3‑1500 U/L (0.05‑25.0 µkat/L)

Determine samples having higher activities via the rerun function. Dilution of samples via the rerun function is a 1:5 dilution. Results from samples diluted using the rerun function are automatically multiplied by a factor of 5.

Lower limits of measurement

Limit of Blank, Limit of Detection and Limit of Quantitation

Limit of Blank

= 3 U/L (0.05 µkat/L)

Limit of Detection

= 3 U/L (0.05 µkat/L)

Limit of Quantitation

= 3 U/L (0.05 µkat/L)

The Limit of Blank, Limit of Detection and Limit of Quantitation were determined in accordance with the CLSI (Clinical and Laboratory Standards Institute) EP17‑A2 requirements.

The Limit of Blank is the 95th percentile value from n ≥ 60 measurements of analyte‑free samples over several independent series. The Limit of Blank corresponds to the activity below which analyte‑free samples are found with a probability of 95 %.

The Limit of Detection is determined based on the Limit of Blank and the standard deviation of low activity samples.

The Limit of Detection corresponds to the lowest analyte activity which can be detected (value above the Limit of Blank with a probability of 95 %).

The Limit of Quantitation is the lowest analyte activity that can be reproducibly measured with a total error of 20 %. It has been determined using low activity α‑amylase samples.

", "Language": "en" }, { "Name": "ExpectedValues", "Value": "

Expected values

Expected values
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

U/L

Serum/plasma

Men/Women

28‑100 U/L

Spontaneously voided urine

Men
Women

16‑491 U/L
21‑447 U/L

α‑amylase/
creatinine quotient

Men
Women

58‑283 U/g
75‑390 U/g

µkat/L*

Serum/plasma

Men/Women

0.47‑1.67 µkat/L

Spontaneously voided urine

Men
Women

0.27‑8.20 µkat/L
0.35‑7.46 µkat/L

α‑amylase/
creatinine quotient

Men
Women

0.97‑4.73 µkat/g
1.25‑6.51 µkat/g

*calculated by unit conversion factor

α‑Amylase/creatinine quotient

To allow for fluctuations in the α‑amylase activity in urine, it is advisable to determine the α‑amylase/creatinine quotient. To do this, determine the α‑amylase activity and creatinine concentration in spontaneously voided urine.

Quotient [µkat/mmol or U/g] =

α‑amylase [µkat/L or U/L]
creatinine [mmol/L or g/L]

Amylase/Creatinine Clearance Ratio (ACCR)
LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

The ACCR is calculated from amylase activity and creatinine concentration. Both the serum and urine samples should be collected at the same time.

ACCR [%] =

urine amylase [U/L] × serum creatinine [mg/L]
serum amylase [U/L] × urine creatinine [mg/L]

× 100

The ACCR is approximately equal to 2‑5 %.

Each laboratory should investigate the transferability of the expected values to its own patient population and if necessary determine its own reference ranges.

", "Language": "en" }, { "Name": "LimitationInterference", "Value": "

Limitations - interference

A slight change in the yellow coloration of solution 2 does not interfere with the performance of the test.

Do not pipette by mouth, and ensure that the reagent does not come into contact with the skin. Saliva and sweat contain α‑amylase!

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 100 U/L.

Serum/plasma

Icterus:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an I index of 60 for conjugated and unconjugated bilirubin (approximate conjugated and unconjugated bilirubin concentration: 1026 µmol/L or 60 mg/dL).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Lipemia (Intralipid):

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an L index of 1500. There is poor correlation between the L index (corresponds to turbidity) and triglycerides concentration.

In rare cases, samples with a combination of elevated turbidity (L‑index) and high Amylase activity may cause a >React or >Abs flag.

Highly turbid and grossly lipemic samples may cause Abs. flags.

Anticoagulants: Interference was found with citrate, fluoride, and EDTA.

LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

Glucose: No significant interference from glucose up to a concentration of 111 mmol/L (2000 mg/dL). Approximately 10 % higher recovery was found at glucose concentrations of 250 mmol/L (4500 mg/dL).

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 5.68 mmol/L (100 mg/dL).

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFBreuer J. Report on the Symposium "Drug effects in Clinical Chemistry Methods". Eur J Clin Chem Clin Biochem 1996;34:385-386.
,
LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Exception: Icodextrin‑based drugs may lead to decreased amylase results.
LREFGokal R, Moberly J, Lindholm B, et al. Metabolic and laboratory effects of icodextrin. Kidney Int 2002;62(81):62-71.

In very rare cases, gammopathy, in particular type IgM (Waldenström’s macroglobulinemia), may cause unreliable results.

LREFBakker AJ, Mücke M. Gammopathy interference in clinical chemistry assays: mechanisms, detection and prevention. Clin Chem Lab Med 2007;45(9):1240-1243.

Urine

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 2.27 mmol/L (40 mg/dL). Approximately 15 % lower recovery was found at ascorbic acid concentrations of 22.7 mmol/L (400 mg/dL).

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 460 U/L.

Hemolysis: No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Phosphate: No significant interference from phosphate up to a concentration of 70 mmol/L (217 mg/dL).

Urea: No significant interference from urea up to a concentration of 1500 mmol/L (9009 mg/dL).

For diagnostic purposes, the results should always be assessed in conjunction with the patient’s medical history, clinical examination and other findings.

ACTION REQUIRED
Special Wash Programming: The use of special wash steps is mandatory when certain test combinations are run together on cobas csystems. All special wash programming necessary for avoiding carry-over is available via the cobas link. The latest version of the carry-over evasion list can be found with the NaOHD/SMS/SCCS Method Sheet for information. For further instructions refer to the operator’s manual.

", "Language": "en" }, { "Name": "OrderInformation", "Value": "

OrderInformation (CC Reagents - cobas + Integra)

Order information

Analyzer(s) on which cobas c pack(s) can be used

08056811190

α‑Amylase EPS ver.2 (750 tests)

System‑ID 2017 001

cobas c 303, cobas c 503

Materials required (but not provided):

10759350190

Calibrator f.a.s. (12 x 3 mL)

Code 20401

05117003190

PreciControl ClinChem Multi 1 (20 x 5 mL)

Code 20391

05947626190

PreciControl ClinChem Multi 1 (4 x 5 mL)

Code 20391

05117216190

PreciControl ClinChem Multi 2 (20 x 5 mL)

Code 20392

05947774190

PreciControl ClinChem Multi 2 (4 x 5 mL)

Code 20392

08063494190

Diluent NaCl 9 % (123 mL)

System‑ID 2906 001

", "Language": "en" }, { "Name": "SystemInformation", "Value": "

System information

AMYL2: ACN 20170 (Serum/plasma)

AMYL2U: ACN 20171 (Urine)

", "Language": "en" }, { "Name": "Handling", "Value": "

Reagent handling

Ready for use

", "Language": "en" }, { "Name": "TestDefinition", "Value": "

Application for serum, plasma and urine

Test definition

Reporting time

10 min

Wavelength (sub/main)

700/415 nm

Reagent pipetting

Diluent (H2O)

R1

78 µL

R3

16 µL

Sample volumes

Sample

Sample dilution

Sample

Diluent (NaCl)

Normal

3.1 µL

Decreased

3.1 µL

20 µL

80 µL

Increased

3.1 µL

For further information about the assay test definitions refer to the application parameters setting screen of the corresponding analyzer and assay.

", "Language": "en" }, { "Name": "StorageStability", "Value": "

Storage and stability

Shelf life at 2‑8 °C:

See expiration date on cobas c pack label.

On‑board in use and refrigerated on the analyzer:

26 weeks

", "Language": "en" }, { "Name": "Calibration", "Value": "

Calibration

Application for serum/plasma (ACN 20170)

Calibrators

S1: H2O

S2: C.f.a.s.

Calibration mode

Linear

Calibration frequency

Automatic full calibration
- after reagent lot change

Full calibration
- as required following quality control procedures

Application for urine (ACN 20171)
Transfer of calibration from serum/plasma application (ACN 20170)

Calibration interval may be extended based on acceptable verification of calibration by the laboratory.

Traceability: This method has been standardized against Roche system reagent using calibrated pipettes together with a manual photometer providing absolute values and substrate-specific absorptivity, ε.

", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "

Specific performance data

Representative performance data on the analyzers are given below. These data represent the performance of the analytical procedure itself.

Results obtained in individual laboratories may differ due to heterogenous sample materials, aging of analyzer components and mixture of reagents running on the analyzer.

", "Language": "en" }, { "Name": "Precision", "Value": "

Precision

Precision was determined using human samples and controls in accordance with the CLSI (Clinical and Laboratory Standards Institute) EP05‑A3 requirements with repeatability (n = 84) and intermediate precision (2 aliquots per run, 2 runs per day, 21 days). Results for repeatability and intermediate precision were obtained on the cobas c 503 analyzer.

Serum/plasma

Repeatability

Mean
U/L

SD
U/L

CV
%

PCCC1c)

76.9

0.438

0.6

PCCC2d)

193

0.831

0.4

Human serum 1

7.38

0.231

3.1

Human serum 2

63.9

0.345

0.5

Human serum 3

509

1.63

0.3

Human serum 4

771

2.67

0.3

Human serum 5

1395

4.13

0.3

Intermediate precision

Mean
U/L

SD
U/L

CV
%

PCCC1

FREFPreciControl ClinChem Multi 1

76.9

0.713

0.9

PCCC2

FREFPreciControl ClinChem Multi 2

194

1.51

0.8

Human serum 1

7.38

0.263

3.6

Human serum 2

63.6

0.409

0.6

Human serum 3

509

2.51

0.5

Human serum 4

771

4.13

0.5

Human serum 5

1395

6.04

0.4

Urine

Repeatability

Mean
U/L

SD
U/L

CV
%

Control 1e)

56.3

0.327

0.6

Control 2e)

180

0.707

0.4

Human urine 1

7.78

0.257

3.3

Human urine 2

263

0.913

0.3

Human urine 3

408

1.13

0.3

Human urine 4

766

1.96

0.3

Human urine 5

1385

3.62

0.3

Intermediate precision

Mean
U/L

SD
U/L

CV
%

Control 1

FREFcommercially available control material

56.3

0.370

0.7

Control 2

FREFcommercially available control material

180

0.801

0.4

Human urine 1

7.74

0.403

5.2

Human urine 2

263

2.09

0.8

Human urine 3

409

10.6

2.6

Human urine 4

767

4.41

0.6

Human urine 5

1385

5.66

0.4

The data obtained on cobas c 503 analyzer(s) are representative for cobas c 303 analyzer(s).

", "Language": "en" }, { "Name": "MethodComparison", "Value": "

Method comparison

Amylase values for human serum, plasma and urine samples obtained on a cobas c 503 analyzer (y) were compared to those determined using the corresponding reagent on a cobas c 501 analyzer (x).

Serum/plasma

Sample size (n) = 85

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.006x − 0.00259 U/L

y = 1.008x − 0.399 U/L

τ = 0.993

r = 1.000

The sample activities were between 10.3 and 1439 U/L.

Urine

Sample size (n) = 67

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.997x + 0.221 U/L

y = 0.996x + 0.571 U/L

τ = 0.985

r = 1.000

The sample activities were between 6.90 and 1467 U/L.

Amylase values for human serum, plasma and urine samples obtained on a cobas c 303 analyzer (y) were compared to those determined using the corresponding reagent on a cobas c 501 analyzer (x).

Serum/plasma

Sample size (n) = 73

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.013x − 0.271 U/L

y = 1.012x − 0.182 U/L

τ = 0.993

r = 1.000

The sample activities were between 9.10 and 1460 U/L.

Urine

Sample size (n) = 71

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 1.014x - 0.186 U/L

y = 1.019x - 0.515 U/L

τ = 0.991

r = 1.000

The sample activities were between 4.80 and 1444 U/L.

", "Language": "en" }, { "Name": "Summary", "Value": "

Summary

Summary
LREFGreiling H, Gressner AM, eds. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3rd ed. Stuttgart/New York: Schattauer Verlag 1995.
,
LREFKeller H, ed. Klinisch-chemische Labordiagnostik für die Praxis, 2nd ed. Stuttgart/New York: Georg Thieme Verlag 1991:354-361.
,
LREFSalt WB II, Schenker S. Amylase - its clinical significance: a review of the literature [Review]. Medicine 1976;55:269-281.
,
LREFSteinberg WM, Goldstein SS, Davies ND, et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985;102:576-580.
,
LREFTietz NW, Huang WY, Rauh DF, et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32(2):301-307.
,
LREFJunge W, Troge B, Klein G, et al. Evaluation of a New Assay for Pancreatic Amylase: Performance Characteristics and Estimation of Reference Intervals. Clin Biochem 1989;22:109-114.
,
LREFRauscher E, von Bülow S, Hägele EO, et al. Ethylidene protected substrate for the assay of human α-amylase. Fresenius Z Anal Chem 1986;324:304-305.
,
LREFKruse-Jarres JD, Hafkenscheid JCM, Hohenwallner W, et al. Evaluation of a New α-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-nitrophenyl-(G1)-α-D-maltoheptaoside as Substrate. J Clin Chem Clin Biochem 1989;27:103-113.
,
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

The α‑amylases (1,4‑α‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4‑α‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ‑specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.

Because of the sparsity of specific clinical symptoms of pancreatic diseases, α‑amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas‑specific enzyme ‑ lipase or pancreatic‑α‑amylase ‑ also be determined.

Numerous methods have been described for the determination of α‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme‑catalyzed subsequent reactions. The kinetic method described here is based on the well‑proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑α,D‑maltoheptaoside (Ethylidene Protected Substrate = EPS) by α‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC. This assay follows the recommendation of the IFCC, but was optimized for performance and stability.

", "Language": "en" }, { "Name": "Reagents", "Value": "

Reagents - working solutions

R1

HEPES: 52.4 mmol/L; sodium chloride: 87 mmol/L; calcium chloride: 0.08 mmol/L; magnesium chloride: 12.6 mmol/L; α‑glucosidase (microbial): ≥ 66.8 µkat/L; pH 7.0 (37 °C); preservatives; stabilizers

R3

HEPES: 52.4 mmol/L; ethylidene‑G7‑PNP: 22 mmol/L; pH 7.0 (37 °C); preservatives; stabilizers

R1 is in position B and R3 is in position C.

", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "

Precautions and warnings

For in vitro diagnostic use for health care professionals. Exercise the normal precautions required for handling all laboratory reagents.

Infectious or microbial waste:
Warning: handle waste as potentially biohazardous material. Dispose of waste according to accepted laboratory instructions and procedures.

Environmental hazards:
Apply all relevant local disposal regulations to determine the safe disposal.

Safety data sheet available for professional user on request.

This kit contains components classified as follows in accordance with the Regulation (EC) No. 1272/2008:

Warning

H317

May cause an allergic skin reaction.

Prevention:

P261

Avoid breathing dust/fume/gas/mist/vapours/spray.

P272

Contaminated work clothing should not be allowed out of the workplace.

P280

Wear protective gloves.

Response:

P333 + P313

If skin irritation or rash occurs: Get medical advice/attention.

P362 + P364

Take off contaminated clothing and wash it before reuse.

Disposal:

P501

Dispose of contents/container to an approved waste disposal plant.

Product safety labeling follows EU GHS guidance.

Contact phone: all countries: +49-621-7590

", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "

Quality control

For quality control, use control materials as listed in the “Order information” section. In addition, other suitable control material can be used.

Serum/plasma:

PreciControl ClinChem Multi 1
PreciControl ClinChem Multi 2

Urine:

Quantitative urine controls are recommended for routine quality control.

The control intervals and limits should be adapted to each laboratory’s individual requirements. It is recommended to perform quality control always after lot calibration and subsequently at least every 26 weeks. Values obtained should fall within the defined limits. Each laboratory should establish corrective measures to be taken if values fall outside the defined limits.

Follow the applicable government regulations and local guidelines for quality control.

", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "

Specimen collection and preparation

Specimen collection and preparation
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.
,
LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

For specimen collection and preparation only use suitable tubes or collection containers.

Only the specimens listed below were tested and found acceptable.
Serum
Plasma: Li‑heparin plasma

The sample types listed were tested with a selection of sample collection tubes that were commercially available at the time of testing, i.e. not all available tubes of all manufacturers were tested. Sample collection systems from various manufacturers may contain differing materials which could affect the test results in some cases. When processing samples in primary tubes (sample collection systems), follow the instructions of the tube manufacturer.

Centrifuge samples containing precipitates before performing the assay.

Urine: Collect urine without additives. α‑Amylase is unstable in acid urine. Assay promptly or adjust pH to alkaline range (just above pH 7) before storage.

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

If stabilizers are added to the sample, the sample index feature must not be used.

See the limitations and interferences section for details about possible sample interferences.

Stability in serum or plasma:

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

7 days at 15‑25 °C

1 month at 2‑8 °C

Stability in urine:

LREFHohenwallner W, Hägele EO, Scholer A, et al. Bestimmung von alpha-Amylase mit p-Nitrophenylmaltoheptaosid als Substrat. Ber Öster Ges Klin Chem 1983;6:101-112.

2 days at 15‑25 °C

10 days at 2‑8 °C

Sample stability claims were established by experimental data by the manufacturer or based on reference literature and only for the temperatures/time frames as stated in the method sheet. It is the responsibility of the individual laboratory to use all available references and/or its own studies to determine specific stability criteria for its laboratory.

", "Language": "en" } ] } }, { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "0003183742122c501", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "12", "DocumentObjectID": "FF00000004875D0E", "DocumentOriginID": "FF000000002DB60E", "MaterialNumbers": [ "03183742122" ], "InstrumentReferences": [ { "ID": "308", "BrandName": "cobas c 311" }, { "ID": "2324", "BrandName": "cobas c 502" }, { "ID": "309", "BrandName": "cobas c 501" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "

Intended use

In vitro test for the quantitative determination of α‑amylase in human serum, plasma and urine on Roche/Hitachi cobas c systems.

", "Language": "en" }, { "Name": "TestPrinciple", "Value": "

Test principle

Test principle
LREFLorentz K. Approved recommendation on IFCC methods for the measurement of catalytic concentration of enzymes. Part 9. IFCC Method for α-Amylase. (1,4-α-D-Glucan 4-Glucanohydrolase, EC 3.2.1.1). Clin Chem Lab Med 1998;36(3):185-203.
,
LREFKurrle-Weitenhiller A, Hölzel W, Engel D, et al. Method for the determination of total and pancreatic α-amylase based on 100 % cleavage of the protected substrate ethylidene-4-nitrophenyl-maltoheptaoside. Clin Chem 1996;42(S6):98.

Enzymatic colorimetric assay acc. to IFCC.

Defined oligosaccharides such as 4,6‑ethylidene‑(G7) p‑nitrophenyl‑(G1)‑α‑D‑maltoheptaoside (ethylidene‑G7PNP) are cleaved under the catalytic action of α‑amylases. The G2PNP, G3PNP and G4PNP fragments so formed are completely hydrolyzed to p‑nitrophenol and glucose by α‑glucosidase.

Simplified reaction scheme:

α‑amylase

5 ethylidene‑G7PNP

FREFPNP p‑nitrophenol
 + 5 H2O

2 ethylidene‑G5 + 2 G2PNP + 2 ethylidene‑G4 + 2 G3PNP +
ethylidene‑G3 + G4PNP

α‑glucosidase

2 G2PNP + 2 G3PNP +
G4PNP + 14 H2O 

  5 PNP + 14 G

FREF G Glucose

The color intensity of the p‑nitrophenol formed is directly proportional to the α‑amylase activity. It is determined by measuring the increase in absorbance.

", "Language": "en" }, { "Name": "MeasuringRange", "Value": "

Limits and ranges

Measuring range

Serum/plasma/urine

3‑1500 U/L (0.05‑25.0 µkat/L)

Determine samples having higher activities via the rerun function. Dilution of samples via the rerun function is a 1:5 dilution. Results from samples diluted using the rerun function are automatically multiplied by a factor of 5.

Lower limits of measurement

Lower detection limit of the test

3 U/L (0.05 µkat/L)

The lower detection limit represents the lowest measurable analyte level that can be distinguished from zero. It is calculated as the value lying three standard deviations above that of the lowest standard (standard 1 + 3 SD, repeatability, n = 21).

", "Language": "en" }, { "Name": "ExpectedValues", "Value": "

Expected values

Expected values
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

Serum/plasma

Men/Women

0.47‑1.67 µkat/L

28‑100 U/L

Spontaneously voided urine

Men
Women

0.27‑8.20 µkat/L
0.35‑7.46 µkat/L

16‑491 U/L
21‑447 U/L

α‑amylase/
creatinine quotient

Men
Women

0.97‑4.73 µkat/g
1.25‑6.51 µkat/g

58‑283 U/g
75‑390 U/g

α‑Amylase/creatinine quotient

To allow for fluctuations in the α‑amylase activity in urine, it is advisable to determine the α‑amylase/creatinine quotient. To do this, determine the α‑amylase activity and creatinine concentration in spontaneously voided urine.

Quotient [U/g or µkat/mmol] =

α‑amylase [U/L or µkat/L]

creatinine [g/L or mmol/L]

Amylase/Creatinine Clearance Ratio (ACCR)

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

The ACCR is calculated from amylase activity and creatinine concentration. Both the serum and urine samples should be collected at the same time.

ACCR [%] =

urine amylase [U/L] × serum creatinine [mg/L]

× 100

serum amylase [U/L] × urine creatinine [mg/L]

The ACCR is approximately equal to 2‑5 %.

Each laboratory should investigate the transferability of the expected values to its own patient population and if necessary determine its own reference ranges.

", "Language": "en" }, { "Name": "LimitationInterference", "Value": "

Limitations - interference

A slight change in the yellow coloration of solution 2 does not interfere with the performance of the test.

Do not pipette by mouth, and ensure that the reagent does not come into contact with the skin. Saliva and sweat contain α‑amylase!

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 100 U/L (1.67 µkat/L).

Serum/plasma

Icterus:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an I index of 60 for conjugated and unconjugated bilirubin (approximate conjugated and unconjugated bilirubin concentration: 1026 µmol/L or 60 mg/dL).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an H index of 500 (approximate hemoglobin concentration: 311 µmol/L or 500 mg/dL).

Lipemia (Intralipid):

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an L index of 1500. There is poor correlation between the L index (corresponds to turbidity) and triglycerides concentration.

In rare cases, samples with a combination of elevated turbidity (L‑index) and high Amylase activity may cause a >React or >Abs flag.

Highly turbid and grossly lipemic samples may cause Abs. flags.

Anticoagulants: Interference was found with citrate, fluoride, and EDTA.

LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

Glucose: No significant interference from glucose up to a concentration of 111 mmol/L (2000 mg/dL). Approximately 10 % higher recovery was found at glucose concentrations of 250 mmol/L (4500 mg/dL).

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 5.68 mmol/L (100 mg/dL).

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFBreuer J. Report on the Symposium "Drug effects in Clinical Chemistry Methods". Eur J Clin Chem Clin Biochem 1996;34:385-386.
,
LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Exception: Icodextrin‑based drugs may lead to decreased amylase results.

LREFGokal R, Moberly J, Lindholm B, et al. Metabolic and laboratory effects of icodextrin. Kidney Int 2002;62(81):62-71.

In very rare cases, gammopathy, in particular type IgM (Waldenström’s macroglobulinemia), may cause unreliable results.

LREFBakker AJ, Mücke M. Gammopathy interference in clinical chemistry assays: mechanisms, detection and prevention. Clin Chem Lab Med 2007;45(9):1240-1243.

Urine

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Ascorbic acid: No significant interference from ascorbic acid up to a concentration of 2.27 mmol/L (40 mg/dL). Approximately 15 % lower recovery was found at ascorbic acid concentrations of 22.7 mmol/L (400 mg/dL).

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 460 U/L (7.68 µkat/L).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to a hemoglobin concentration of 311 µmol/L or 500 mg/dL.

Phosphate: No significant interference from phosphate up to a concentration of 70 mmol/L (217 mg/dL).

Urea: No significant interference from urea up to a concentration of 1500 mmol/L (9009 mg/dL).

For diagnostic purposes, the results should always be assessed in conjunction with the patient’s medical history, clinical examination and other findings.

ACTION REQUIRED
Special Wash Programming: The use of special wash steps is mandatory when certain test combinations are run together on Roche/Hitachi cobas c systems. The latest version of the carry‑over evasion list can be found with the NaOHD-SMS-SmpCln1+2-SCCS Method Sheets. For further instructions refer to the operator’s manual. cobas c 502 analyzer: All special wash programming necessary for avoiding carry‑over is available via the cobas link, manual input is required in certain cases.

Where required, special wash/carry‑over evasion programming must be implemented prior to reporting results with this test.

", "Language": "en" }, { "Name": "OrderInformation", "Value": "

OrderInformation (CC Reagents - cobas + Integra)

Order information

Analyzer(s) on which cobas c pack(s) can be used

03183742 122

α‑Amylase EPS ver.2 (300 tests)

System‑ID 07 6609 7

Roche/Hitachi cobas c 311, cobas c 501/502

Materials required (but not provided):

10759350 190

Calibrator f.a.s. (12 x 3 mL)

Code 401

10759350 360

Calibrator f.a.s. (12 x 3 mL, for USA)

Code 401

12149435 122

Precinorm U plus (10 x 3 mL)

Code 300

12149435 160

Precinorm U plus (10 x 3 mL, for USA)

Code 300

12149443 122

Precipath U plus (10 x 3 mL)

Code 301

12149443 160

Precipath U plus (10 x 3 mL, for USA)

Code 301

05117003 190

PreciControl ClinChem Multi 1 (20 x 5 mL)

Code 391

05947626 190

PreciControl ClinChem Multi 1 (4 x 5 mL)

Code 391

05947626 160

PreciControl ClinChem Multi 1 (4 x 5 mL, for USA)

Code 391

05117216 190

PreciControl ClinChem Multi 2 (20 x 5 mL)

Code 392

05947774 190

PreciControl ClinChem Multi 2 (4 x 5 mL)

Code 392

05947774 160

PreciControl ClinChem Multi 2 (4 x 5 mL, for USA)

Code 392

04489357 190

Diluent NaCl 9 % (50 mL)

System‑ID 07 6869 3

", "Language": "en" }, { "Name": "SystemInformation", "Value": "

System information

For cobas c 311/501 analyzers:

AMYL2: ACN 570

SAMY2: ACN 566 (STAT, reaction time: 7)

For cobas c 502 analyzer:

AMYL2: ACN 8570

SAMY2: ACN 8566 (STAT, reaction time: 7)

", "Language": "en" }, { "Name": "Handling", "Value": "

Reagent handling

Ready for use

", "Language": "en" }, { "Name": "TestDefinition", "Value": "

Application for serum, plasma and urine

cobas c 311 test definition

Assay type

Rate A

Reaction time /
Assay points

10 / 22‑32
(STAT 7/ 22‑32)

Wavelength (sub/main)

700/415 nm

Reaction direction

Increase

Unit

U/L (µkat/L)

Reagent pipetting

Diluent (H2O)

R1

100 µL

R2

20 µL

Sample volumes

Sample

Sample dilution

Sample

Diluent (NaCl)

Normal

4 µL

Decreased

8 µL

15 µL

135 µL

Increased

4 µL

cobas c 501 test definition

Assay type

Rate A

Reaction time /
Assay points

10 / 30‑47
(STAT 7 / 30‑47)

Wavelength (sub/main)

700/415 nm

Reaction direction

Increase

Unit

U/L (µkat/L)

Reagent pipetting

Diluent (H2O)

R1

100 µL

R2

20 µL

Sample volumes

Sample

Sample dilution

Sample

Diluent (NaCl)

Normal

4 µL

Decreased

8 µL

15 µL

135 µL

Increased

4 µL

cobas c 502 test definition

Assay type

Rate A

Reaction time /
Assay points

10 / 30‑47
(STAT 7 / 30‑47)

Wavelength (sub/main)

700/415 nm

Reaction direction

Increase

Unit

U/L (µkat/L)

Reagent pipetting

Diluent (H2O)

R1

100 µL

R2

20 µL

Sample volumes

Sample

Sample dilution

Sample

Diluent (NaCl)

Normal

4 µL

Decreased

8 µL

15 µL

135 µL

Increased

8 µL

", "Language": "en" }, { "Name": "StorageStability", "Value": "

Storage and stability

AMYL2

Shelf life at 2‑8 °C:

See expiration date on cobas c pack label.

On‑board in use and refrigerated on the analyzer:

12 weeks

Diluent NaCl 9 %

Shelf life at 2‑8 °C:

See expiration date on cobas c pack label.

On‑board in use and refrigerated on the analyzer:

12 weeks

", "Language": "en" }, { "Name": "Calibration", "Value": "

Calibration

Calibrators

S1: H2O

S2: C.f.a.s.

Calibration mode

Linear

Calibration frequency

2‑point calibration
• after reagent lot change
• as required following quality control procedures

Calibration interval may be extended based on acceptable verification of calibration by the laboratory.

Traceability: This method has been standardized against Roche system reagent using calibrated pipettes together with a manual photometer providing absolute values and substrate-specific absorptivity, ε.

", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "

Specific performance data

Representative performance data on the analyzers are given below. Results obtained in individual laboratories may differ.

", "Language": "en" }, { "Name": "Precision", "Value": "

Precision

Precision was determined using human samples and controls in an internal protocol with repeatability (n = 21) and intermediate precision (3 aliquots per run, 1 run per day, 21 days). The following results were obtained:

Serum/plasma

Repeatability

Mean

U/L (µkat/L)

SD

U/L (µkat/L)

CV

%

Precinorm U

83.2 (1.39)

0.8 (0.01)

0.9

Precipath U

182 (3.09)

1 (0.02)

0.6

Human serum 1

34.5 (0.576)

0.4 (0.007)

1.2

Human serum 2

97.9 (1.63)

0.7 (0.01)

0.7

Intermediate precision

Mean

U/L (µkat/L)

SD

U/L (µkat/L)

CV

%

Precinorm U

84.0 (1.40)

1.1 (0.02)

1.3

Precipath U

184 (3.08)

3 (0.05)

1.5

Human serum 3

35.1 (0.586)

0.9 (0.015)

2.4

Human serum 4

98.9 (1.65)

1.6 (0.03)

1.6

Urine

Repeatability

Mean

U/L (µkat/L)

SD

U/L (µkat/L)

CV

%

Control level 1

50.6 (0.845)

0.5 (0.008)

0.9

Control level 2

164 (2.74)

1 (0.02)

0.6

Urine 1

21.4 (0.357)

0.2 (0.003)

1.1

Urine 2

68.5 (1.14)

0.7 (0.01)

0.9

Intermediate precision

Mean

U/L (µkat/L)

SD

U/L (µkat/L)

CV

%

Control level 1

51.8 (0.865)

0.9 (0.015)

1.7

Control level 2

168 (2.81)

2 (0.03)

1.1

Urine 3

24.5 (0.409)

0.5 (0.008)

1.9

Urine 4

67.0 (1.12)

2.8 (0.05)

4.2

The data obtained on cobas c 501 analyzer(s) are representative for cobas c 311 analyzer(s).

", "Language": "en" }, { "Name": "MethodComparison", "Value": "

Method comparison

Amylase values for human serum, plasma and urine samples obtained on a Roche/Hitachi cobas c 501 analyzer (y) were compared with those determined using the corresponding reagent on a Roche/Hitachi 917 analyzer (x).

Serum/plasma

Sample size (n) = 79

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.999x + 2.83 U/L

y = 0.998x + 4.75 U/L

τ = 0.969

r = 0.998

The sample activities were between 51.7 and 1409 U/L (0.863 and 23.5 µkat/L).

Urine

Sample size (n) = 88

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

Linear regression

y = 0.986x + 0.423 U/L

y = 0.982x + 2.03 U/L

τ = 0.987

r = 1.000

The sample activities were between 33.6 and 1248 U/L (0.561 and 20.8 µkat/L).

The data obtained on cobas c 501 analyzer(s) are representative for cobas c 311 analyzer(s).

", "Language": "en" }, { "Name": "Summary", "Value": "

Summary

Summary
LREFGreiling H, Gressner AM, eds. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3rd ed. Stuttgart/New York: Schattauer Verlag 1995.
,
LREFKeller H, ed. Klinisch-chemische Labordiagnostik für die Praxis, 2nd ed. Stuttgart/New York: Georg Thieme Verlag 1991:354-361.
,
LREFSalt WB II, Schenker S. Amylase - its clinical significance: a review of the literature [Review]. Medicine 1976;55:269-281.
,
LREFSteinberg WM, Goldstein SS, Davies ND, et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985;102:576-580.
,
LREFTietz NW, Huang WY, Rauh DF, et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32(2):301-307.
,
LREFJunge W, Troge B, Klein G, et al. Evaluation of a New Assay for Pancreatic Amylase: Performance Characteristics and Estimation of Reference Intervals. Clin Biochem 1989;22:109-114.
,
LREFRauscher E, von Bülow S, Hägele EO, et al. Ethylidene protected substrate for the assay of human α-amylase. Fresenius Z Anal Chem 1986;324:304-305.
,
LREFKruse-Jarres JD, Hafkenscheid JCM, Hohenwallner W, et al. Evaluation of a New α-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-nitrophenyl-(G1)-α-D-maltoheptaoside as Substrate. J Clin Chem Clin Biochem 1989;27:103-113.
,
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

The α‑amylases (1,4‑α‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4‑α‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ‑specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.

Because of the sparsity of specific clinical symptoms of pancreatic diseases, α‑amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas‑specific enzyme ‑ lipase or pancreatic‑α‑amylase ‑ also be determined.

Numerous methods have been described for the determination of α‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme‑catalyzed subsequent reactions. The kinetic method described here is based on the well‑proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑α,D‑maltoheptaoside (Ethylidene Protected Substrate = EPS) by α‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC. This assay follows the recommendation of the IFCC, but was optimized for performance and stability.

", "Language": "en" }, { "Name": "Reagents", "Value": "

Reagents - working solutions

R1

HEPES: 52.4 mmol/L; sodium chloride: 87 mmol/L; calcium chloride: 0.08 mmol/L; magnesium chloride: 12.6 mmol/L; α‑glucosidase (microbial): ≥ 66.8 µkat/L; pH 7.0 (37 °C); preservatives; stabilizers

R2

HEPES: 52.4 mmol/L; ethylidene‑G7‑PNP: 22 mmol/L; pH 7.0 (37 °C); preservatives; stabilizers

R1 is in position B and R2 is in position C.

", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "

Precautions and warnings

For in vitro diagnostic use for health care professionals. Exercise the normal precautions required for handling all laboratory reagents.

Infectious or microbial waste:
Warning: handle waste as potentially biohazardous material. Dispose of waste according to accepted laboratory instructions and procedures.

Environmental hazards:
Apply all relevant local disposal regulations to determine the safe disposal.

Safety data sheet available for professional user on request.

For USA: Caution: Federal law restricts this device to sale by or on the order of a physician.

This kit contains components classified as follows in accordance with the Regulation (EC) No. 1272/2008:

Warning

H317

May cause an allergic skin reaction.

Prevention:

P261

Avoid breathing dust/fume/gas/mist/vapours/spray.

P272

Contaminated work clothing should not be allowed out of the workplace.

P280

Wear protective gloves.

Response:

P333 + P313

If skin irritation or rash occurs: Get medical advice/attention.

P362 + P364

Take off contaminated clothing and wash it before reuse.

Disposal:

P501

Dispose of contents/container to an approved waste disposal plant.

Product safety labeling follows EU GHS guidance.

", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "

Quality control

For quality control, use control materials as listed in the \"Order information\" section.

In addition, other suitable control material can be used.

The control intervals and limits should be adapted to each laboratory’s individual requirements. Values obtained should fall within the defined limits. Each laboratory should establish corrective measures to be taken if values fall outside the defined limits.

Follow the applicable government regulations and local guidelines for quality control.

", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "

Specimen collection and preparation

Specimen collection and preparation
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.
,
LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

For specimen collection and preparation only use suitable tubes or collection containers.

Only the specimens listed below were tested and found acceptable.
Serum
Plasma: Li‑heparin plasma.

The sample types listed were tested with a selection of sample collection tubes that were commercially available at the time of testing, i.e. not all available tubes of all manufacturers were tested. Sample collection systems from various manufacturers may contain differing materials which could affect the test results in some cases. When processing samples in primary tubes (sample collection systems), follow the instructions of the tube manufacturer.

Centrifuge samples containing precipitates before performing the assay.

See the limitations and interferences section for details about possible sample interferences.

Sample stability claims were established by experimental data by the manufacturer or based on reference literature and only for the temperatures/time frames as stated in the method sheet. It is the responsibility of the individual laboratory to use all available references and/or its own studies to determine specific stability criteria for its laboratory.

Urine: Collect urine without additives. α‑Amylase is unstable in acid urine. Assay promptly or adjust pH to alkaline range (just above pH 7) before storage.

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

Stability in serum or plasma:

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

7 days at 15‑25 °C

1 month at 2‑8 °C

Stability in urine:

LREFHohenwallner W, Hägele EO, Scholer A, et al. Bestimmung von alpha-Amylase mit p-Nitrophenylmaltoheptaosid als Substrat. Ber Öster Ges Klin Chem 1983;6:101-112.

2 days at 15‑25 °C

10 days at 2‑8 °C

", "Language": "en" } ] } }, { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "0003183742122COIN", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "8", "DocumentObjectID": "FF00000004878F0E", "DocumentOriginID": "FF00000000C01C0E", "MaterialNumbers": [ "03183742122" ], "InstrumentReferences": [ { "ID": "302", "BrandName": "COBAS INTEGRA 400 plus" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "

Intended use

In vitro test for the quantitative determination of the catalytic activity of α‑amylase (1,4‑α‑D‑glucan: glucanohydrolase; EC 3.2.1.1) in human serum, plasma, and urine on COBAS INTEGRA systems.

", "Language": "en" }, { "Name": "TestPrinciple", "Value": "

Test principle

Test principle
LREFLorentz K. Approved recommendation on IFCC methods for the measurement of catalytic concentration of enzymes. Part 9. IFCC Method for α-Amylase. (1,4-α-D-Glucan 4-Glucanohydrolase, EC 3.2.1.1). Clin Chem Lab Med 1998;36(3):185-203.
,
LREFKurrle-Weittenhiller A, Hölzel W, Engel D, et al. Method for the determination of total and pancreatic α-amylase based on 100 % cleavage of the protected substrate ethylidiene-4-nitrophenyl-maltoheptaoside. Clin Chem 1996;42(S6):S98.

Enzymatic colorimetric assay acc. to IFCC.

Defined oligosaccharides such as 4,6‑ethylidene-(G7)-p‑nitrophenyl-(G1)-α,D‑maltoheptaoside (ethylidene‑G7PNP) are cleaved under the catalytic action of α‑amylases. The G2PNP, G3PNP and G4PNP fragments so formed are completely hydrolyzed to p‑nitrophenol and glucose by α‑glucosidase.

Simplified reaction scheme:

5 ethylidene‑G7PNP

FREFPNP = p‑nitrophenol
 + 5 H2O

α‑amylase

2 ethylidene‑G5 + 2 G2PNP

+ 2 ethylidene‑G4 + 2 G3PNP + ethylidene‑G3 + G4PNP

2 G2PNP + 2 G3PNP + G4PNP + 14 H2O

α-glucosidase

5 PNP + 14 G

FREFG = Glucose

The color intensity of the p‑nitrophenol formed is directly proportional to the α‑amylase activity. It is determined by measuring the increase in absorbance at 409 nm.

", "Language": "en" }, { "Name": "MeasuringRange", "Value": "

Limits and ranges

Measuring range

Serum/plasma/urine
3‑2000 U/L (0.05‑33 µkat/L)

Determine samples having higher activities via the rerun function. Dilution of samples via the rerun function is a 1:5 dilution. Results from samples diluted using the rerun function are automatically multiplied by a factor of 5.

Lower limits of measurement

Lower detection limit of the test:
3 U/L (0.05 µkat/L)

The lower detection limit represents the lowest measurable analyte level that can be distinguished from zero. It is calculated as the value lying 3 standard deviations above that of a zero sample (zero sample + 3 SD, repeatability, n = 21).

", "Language": "en" }, { "Name": "ExpectedValues", "Value": "

Expected values

Expected values
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

Serum/plasma

Men/women

28‑100 U/L

(0.47‑1.67 μkat/L)

Spontaneously voided urine

Men

16‑491 U/L

(0.27‑8.20 μkat/L)

Women

21‑447 U/L

(0.35‑7.46 μkat/L)

α‑Amylase/creatinine quotient

Men

58‑283 U/g

(0.97‑4.73 μkat/g)

Women

75‑390 U/g

(1.25‑6.51 μkat/g)

α‑Amylase/creatinine quotient

To allow for fluctuations in the α‑amylase activity in urine, it is advisable to determine the α‑amylase/creatinine quotient. To do this, determine the α‑amylase activity and creatinine concentration in spontaneously voided urine.

Quotient [U/g or µkat/mmol] =

α‑amylase [U/L or µkat/L]
creatinine [g/L or mmol/L]

Amylase/Creatinine Clearance Ratio (ACCR)
LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

The ACCR is calculated from amylase activity and creatinine concentration. Both the serum and urine samples should be collected at the same time.

ACCR [%] =

urine amylase [U/L] × serum creatinine [mg/L]
serum amylase [U/L] × urine creatinine [mg/L]

× 100

ACCR is approximately equal to 2‑5 %.

Each laboratory should investigate the transferability of the expected values to its own patient population and if necessary determine its own reference ranges.

", "Language": "en" }, { "Name": "LimitationInterference", "Value": "

Limitations - interference

Do not pipette by mouth, and ensure that the reagent does not come into contact with the skin. (Saliva and sweat contain α‑amylase!)

Criterion: Recovery within ± 10 % of initial value.

Serum/plasma

Icterus:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an I index of 52 for conjugated bilirubin and 76 for unconjugated bilirubin (approximate conjugated bilirubin concentration: 889 µmol/L or 52 mg/dL; approximate unconjugated bilirubin concentration: 1300 µmol/L or 76 mg/dL).

Hemolysis:

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an H index of 260 (approximate hemoglobin concentration: 161 µmol/L or 260 mg/dL).

Lipemia (Intralipid):

LREFGlick MR, Ryder KW, Jackson SA. Graphical Comparisons of Interferences in Clinical Chemistry Instrumentation. Clin Chem 1986;32:470-475.
No significant interference up to an L index of 2200. There is poor correlation between the L index (corresponds to turbidity) and triglycerides concentration.

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFBreuer J. Report on the Symposium "Drug effects in Clinical Chemistry Methods". Eur J Clin Chem Clin Biochem 1996;34:385-386.
,
LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.
Exceptions: Icodextrin-based drugs may cause artificially low amylase results.
LREFGokal R, Moberly J, Lindholm B, et al. Metabolic and laboratory effects of icodextrin. Kidney Int 2002;62(81):62-71.

Anticoagulants: Interference was found with citrate and fluoride.

LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

In very rare cases, gammopathy, in particular type IgM (Waldenström’s macroglobulinemia), may cause unreliable results.

LREFBakker AJ, Mücke M. Gammopathy interference in clinical chemistry assays: mechanisms, detection and prevention. Clin Chem Lab Med 2007;45(9):1240-1243.

Urine

Drugs: No interference was found at therapeutic concentrations using common drug panels.

LREFSonntag O, Scholer A. Drug interference in clinical chemistry: recommendation of drugs and their concentrations to be used in drug interference studies. Ann Clin Biochem 2001;38:376-385.

Criterion: Recovery within ± 10 % of initial value at an amylase activity of 460 U/L (7.68 µkat/L).

Hemolysis: No significant interference up to a hemoglobin concentration of of 311 µmol/L (500 mg/dL).

Phosphate: No significant interference from phosphate up to a concentration of 70 mmol/L (217 mg/dL).

Urea: No significant interference from urea up to a concentration of 1500 mmol/L (9009 mg/dL).

For diagnostic purposes, the results should always be assessed in conjunction with the patient’s medical history, clinical examination and other findings.

ACTION REQUIRED
Special Wash Programming: The use of special wash steps is mandatory when certain test combinations are run together on COBAS INTEGRA analyzers. Refer to the CLEAN Method Sheet for further instructions and for the latest version of the Extra wash cycle list.
Where required, special wash/carry-over evasion programming must be implemented prior to reporting results with this test.

", "Language": "en" }, { "Name": "OrderInformation", "Value": "

Orderinformation_INT

Order information

Analyzer(s) on which cobas c pack(s) can be used

03183742 122

α-Amylase EPS ver.2 (300 tests)

System-ID 07 6609 7

COBAS INTEGRA 400 plus

Materials required (but not provided):

10759350 190

Calibrator f.a.s. (12 × 3 mL)

System-ID 07 3718 6

10759350 360

Calibrator f.a.s. (12 × 3 mL, for USA)

System-ID 07 3718 6

12149435 122

Precinorm U plus (10 × 3 mL)

System-ID 07 7999 7

12149435 160

Precinorm U plus (10 × 3 mL, for USA)

System-ID 07 7999 7

12149443 122

Precipath U plus (10 × 3 mL)

System-ID 07 8000 6

12149443 160

Precipath U plus (10 × 3 mL, for USA)

System-ID 07 8000 6

05117003 190

PreciControl ClinChem Multi 1 (20 × 5 mL)

System-ID 07 7469 3

05947626 190

PreciControl ClinChem Multi 1 (4 × 5 mL)

System-ID 07 7469 3

05947626 160

PreciControl ClinChem Multi 1 (4 × 5 mL, for USA)

System-ID 07 7469 3

05117216 190

PreciControl ClinChem Multi 2 (20 × 5 mL)

System-ID 07 7470 7

05947774 190

PreciControl ClinChem Multi 2 (4 × 5 mL)

System-ID 07 7470 7

05947774 160

PreciControl ClinChem Multi 2 (4 × 5 mL, for USA)

System-ID 07 7470 7

", "Language": "en" }, { "Name": "SystemInformation", "Value": "

System information

Test AMYL2, test ID 0‑609 (serum, plasma)

Test AMYU2, test ID 0‑509 (urine)

", "Language": "en" }, { "Name": "Handling", "Value": "

Reagent handling

Ready for use

", "Language": "en" }, { "Name": "TestDefinition", "Value": "

Application for serum, plasma and urine

Test definition

Measuring mode

Absorbance

Abs. calculation mode

Kinetic

Reaction mode

R1‑S‑SR

Reaction direction

Increase

Wavelength A/B

409/659 nm

Calc. first/last

50/69

Unit

U/L

Pipetting parameters

Serum/plasma/urine

Diluent (H2O)

R1

100 µL

Sample

4 µL

4 µL

SR

20 µL

Total volume

128 µL

", "Language": "en" }, { "Name": "StorageStability", "Value": "

Storage and stability

Shelf life at 2‑8 °C

See expiration date on cobas c pack label

On-board in use at 10‑15 °C

12 weeks

", "Language": "en" }, { "Name": "Calibration", "Value": "

Calibration

Calibration

Calibrator

Calibrator f.a.s.

Use deionized water as zero calibrator.

Calibration mode

Linear regression

Calibration replicate

Duplicate recommended

Calibration interval

Each lot and as required following quality control procedures

Calibration interval may be extended based on acceptable verification of calibration by the laboratory.

Traceability: This method has been standardized manually against Roche reagent according to IFCC.

", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "

Specific performance data

Representative performance data on the COBAS INTEGRA analyzers are given below. Results obtained in individual laboratories may differ.

", "Language": "en" }, { "Name": "Precision", "Value": "

Precision

Precision was determined using human samples and controls in an internal protocol with repeatability (n = 21) and intermediate precision (1 aliquot per run, 1 run per day, 21 days). The following results were obtained:

Serum/plasma

Repeatability

Level 1

Level 2

Mean

76 U/L
(1.3 µkat/L)

192 U/L
(3.2 µkat/L)

CV

1.4 %

1.2 %

Intermediate precision

Level 1

Level 2

Mean

73 U/L
(1.2 µkat/L)

181 U/L
(3.0 µkat/L)

CV

1.4 %

1.4 %

Urine

Repeatability

Level 1

Level 2

Mean

39.4 U/L
(0.66 µkat/L)

201 U/L
(3.4 µkat/L)

CV

0.8 %

0.4 %

Intermediate precision

Level 1

Level 2

Mean

36.7 U/L
(0.61 µkat/L)

189 U/L
(3.2 µkat/L)

CV

1.0 %

1.0 %

", "Language": "en" }, { "Name": "MethodComparison", "Value": "

Method comparison

α‑Amylase values for human serum, plasma and urine samples obtained on a COBAS INTEGRA 700 analyzer using the COBAS INTEGRA α‑Amylase EPS ver.2 (AMYL2) reagent (y) were compared with those determined using the corresponding reagent on a Roche/Hitachi 917 analyzer (x) and to the previous reagent (AMYLL) on a COBAS INTEGRA 700 analyzer (x).

Serum/plasma

Roche/Hitachi 917 analyzer

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

y = 0.98× + 0.51 U/L

т = 0.987

SD (md 95) = 5.57

Sample size (n) = 64

Linear regression

y = 1.00× - 1.28 U/L

r = 1.000

Sy.x = 5.59

The sample activities were between 22 and 1900 U/L (0.37 and 31.7 μkat/L).

COBAS INTEGRA 700 analyzer

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

y = 0.98× + 1.72 U/L

т = 0.982

SD (md 95) = 12.22

Sample size (n) = 64

Linear regression

y = 0.97× + 3.01 U/L

r = 1.000

Sy.x = 5.71

The sample activities were between 22 and 1930 U/L (0.37 and 32.2 μkat/L).

Urine

Roche/Hitachi 917 analyzer

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

y = 0.98× - 0.32 U/L

т = 0.988

SD (md 95) = 17.3

Sample size (n) = 59

Linear regression

y = 0.99× - 1.03 U/L

r = 1.000

Sy.x = 6.54

The sample activities were between 0.66 and 1767 U/L (0.01 and 29.5 μkat/L).

COBAS INTEGRA 700 analyzer

Passing/Bablok

LREFBablok W, Passing H, Bender R, et al. A general regression procedure for method transformation. Application of linear regression procedures for method comparison studies in clinical chemistry, Part III. J Clin Chem Clin Biochem 1988 Nov;26(11):783-790.

y = 0.96× + 0.54 U/L

т = 0.991

SD (md 95) = 18.6

Sample size (n) = 59

Linear regression

y = 0.95× + 1.92 U/L

r = 1.000

Sy.x = 6.28

The sample activities were between 0.64 and 1853 U/L (0.01 and 30.9 μkat/L).

", "Language": "en" }, { "Name": "Summary", "Value": "

Summary

Summary
LREFGreiling H, Gressner AM, eds. Lehrbuch der Klinischen Chemie und Pathobiochemie, 3rd ed. Stuttgart/New York: Schattauer Verlag 1995.
,
LREFKeller H, ed. Klinisch-chemische Labordiagnostik für die Praxis, 2nd ed. Stuttgart/New York: Georg Thieme Verlag 1991:354-361.
,
LREFSalt WB II, Schenker S. Amylase - its clinical significance: a review of the literature [Review]. Medicine 1976;55:269-281.
,
LREFSteinberg WM, Goldstein SS, Davies ND, et al. Diagnostic assays in acute pancreatitis [Review]. Ann Intern Med 1985;102:576-580.
,
LREFTietz NW, Huang WY, Rauh DF et al. Laboratory tests in the differential diagnosis of hyperamylasemia. Clin Chem 1986;32:301-307.
,
LREFJunge W, Troge B, Klein G, et al. Evaluation of a New Assay for Pancreatic Amylase: Performance Characteristics and Estimation of Reference Intervals. Clin Biochem 1989;22:109-114.
,
LREFRauscher E, von Bülow S, Hägele EO, et al. Ethylidene protected substrate for the assay of human α-amylase. Fresenius Z Anal Chem 1986;324:304-305.
,
LREFKruse-Jarres JD, Hafkenscheid JCM, Hohenwallner W, et al. Evaluation of a New α-Amylase Assay Using 4,6-Ethylidene-(G7)-1-4-nitrophenyl-(G1)-α-D-maltoheptaoside as Substrate. J Clin Chem Clin Biochem 1989;27:103-113.
,
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.

The α‑amylases (1,4‑α‑D‑glucanohydrolases, EC 3.2.1.1) catalyze the hydrolytic degradation of polymeric carbohydrates such as amylose, amylopectin and glycogen by cleaving 1,4‑α‑glucosidic bonds. In polysaccharides and oligosaccharides, several glycosidic bonds are hydrolyzed simultaneously. Maltotriose, the smallest such unit, is converted into maltose and glucose, albeit very slowly. Two types of α‑amylases can be distinguished, the pancreatic type (P‑type) and the salivary type (S‑type). Whereas the P‑type can be attributed almost exclusively to the pancreas and is therefore organ-specific, the S‑type can originate from a number of sites. As well as appearing in the salivary glands it can also be found in tears, sweat, human milk, amniotic fluid, the lungs, testes and the epithelium of the fallopian tube.

Because of the sparsity of specific clinical symptoms of pancreatic diseases, α-amylase determinations are of considerable importance in pancreatic diagnostics. They are mainly used in the diagnosis and monitoring of acute pancreatitis. Hyperamylasemia does not, however, only occur with acute pancreatitis or in the inflammatory phase of chronic pancreatitis, but also in renal failure (reduced glomerular filtration), tumors of the lungs or ovaries, pulmonary inflammation, diseases of the salivary gland, diabetic ketoacidosis, cerebral trauma, surgical interventions or in the case of macroamylasemia. To confirm pancreatic specificity, it is recommended that an additional pancreas-specific enzyme ‑ lipase or pancreatic-α‑amylase ‑ also be determined.

Numerous methods have been described for the determination of α‑amylase. These either determine the decrease in the amount of substrate viscometrically, turbidimetrically, nephelometrically and amyloclastically or measure the formation of degradation products saccharogenically or kinetically with the aid of enzyme-catalyzed subsequent reactions. The kinetic method described here is based on the well-proven cleavage of 4,6‑ethylidene‑(G7)‑1,4‑nitrophenyl‑(G1)‑α,D‑maltoheptaoside (Ethylidene Protected Substrate = EPS) by α‑amylase and subsequent hydrolysis of all the degradation products to p‑nitrophenol with the aid of α‑glucosidase (100 % chromophore liberation). The results of this method correlate with those obtained by HPLC.

", "Language": "en" }, { "Name": "Reagents", "Value": "

Reagents - working solutions

R1

HEPES: 52.4 mmol/L; sodium chloride: 87 mmol/L; calcium chloride: 0.08 mmol/L; magnesium chloride: 12.6 mmol/L; α‑glucosidase (microbial): ≥ 66.8 µkat/L; pH 7.0 (37 °C); detergent; stabilizers

SR

HEPES: 52.4 mmol/L; ethylidene‑G7‑PNP: 22 mmol/L; pH 7.0 (37 °C); detergent; stabilizers

R1 is in position B and SR is in position C.

", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "

Precautions and warnings

For in vitro diagnostic use for health care professionals. Exercise the normal precautions required for handling all laboratory reagents.

Infectious or microbial waste:
Warning: handle waste as potentially biohazardous material. Dispose of waste according to accepted laboratory instructions and procedures.

Environmental hazards:
Apply all relevant local disposal regulations to determine the safe disposal.

Safety data sheet available for professional user on request.

For USA: Caution: Federal law restricts this device to sale by or on the order of a physician.

This kit contains components classified as follows in accordance with the Regulation (EC) No. 1272/2008:

Warning

H317

May cause an allergic skin reaction.

Prevention:

P261

Avoid breathing dust/fume/gas/mist/vapours/spray.

P272

Contaminated work clothing should not be allowed out of the workplace.

P280

Wear protective gloves.

Response:

P333 + P313

If skin irritation or rash occurs: Get medical advice/attention.

P362 + P364

Take off contaminated clothing and wash it before reuse.

Disposal:

P501

Dispose of contents/container to an approved waste disposal plant.

Product safety labeling follows EU GHS guidance.

", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "

Quality control

Quality control serum, plasma

Precinorm U plus or PreciControl ClinChem Multi 1

Precipath U plus or PreciControl ClinChem Multi 2

Quality control urine

Quantitative urine controls are recommended for routine quality control.

Control interval

24 hours recommended

Control sequence

User defined

Control after calibration

Recommended

For quality control, use control materials as listed in the “Order information” section. In addition, other suitable control material can be used.

The control intervals and limits should be adapted to each laboratory’s individual requirements. Values obtained should fall within the defined limits. Each laboratory should establish corrective measures to be taken if values fall outside the defined limits.

Follow the applicable government regulations and local guidelines for quality control.

", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "

Specimen collection and preparation

Specimen collection and preparation
LREFJunge W, Wortmann W, Wilke B, et al. Development and evaluation of assays for the determination of total and pancreatic amylase at 37°C according to the principle recommended by the IFCC. Clin Biochem 2001;34:607-615. Erratum Clin Biochem 2003;36:161.
,
LREFYoung DS. Effects of Preclinical Variables on Clinical Laboratory Tests. AACC Press 1997, 2nd edition 1997.

For specimen collection and preparation only use suitable tubes or collection containers.

Only the specimens listed below were tested and found acceptable:
Serum
Plasma: Heparin (Li‑, Na‑, NH4+‑) or EDTA (K2‑, K3‑) plasma

EDTA plasma values are approximately 5‑10 % lower than serum values.

The sample types listed were tested with a selection of sample collection tubes that were commercially available at the time of testing, i.e. not all available tubes of all manufacturers were tested. Sample collection systems from various manufacturers may contain differing materials which could affect the test results in some cases. When processing samples in primary tubes (sample collection systems), follow the instructions of the tube manufacturer.

Urine: Collect urine without additives. α‑Amylase is unstable in acid urine. Assay promptly or adjust pH to alkaline range (just above pH 7) before storage.

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

See the limitations and interferences section for details about possible sample interferences.

Centrifuge samples containing precipitates before performing the assay.

Stability in serum:

LREFTietz NW, ed. Clinical Guide to Laboratory Tests, 3rd ed. Philadelphia PA: WB Saunders Company 1995;46-51.

7 days at 15‑25 °C

1 month at 2‑8 °C

Stability in urine:

LREFHohenwallner W, Hägele EO, Scholer A, et al. Bestimmung von alpha-Amylase mit p-Nitrophenylmaltoheptaosid als Substrat. Ber Öster Ges Klin Chem 1983;6:101-112.

2 days at 15‑25 °C

10 days at 2‑8 °C

Sample stability claims were established by experimental data by the manufacturer or based on reference literature and only for the temperatures/time frames as stated in the method sheet. It is the responsibility of the individual laboratory to use all available references and/or its own studies to determine specific stability criteria for its laboratory.

", "Language": "en" } ] } }, { "ProductSpecVariant": { "MetaData": { "DocumentMaterialNumber": "08542732001", "ProductName": "AMYL2", "ProductLongName": "α-Amylase EPS ver.2", "Language": "en", "DocumentVersion": "1", "DocumentObjectID": "FF00000004E8360E", "DocumentOriginID": "FF0000000274CF0E", "MaterialNumbers": [ "05167027188" ], "InstrumentReferences": [ { "ID": "2492", "BrandName": "cobas c 702" }, { "ID": "310", "BrandName": "cobas c 701" } ], "DisclaimerText": "Product information shown on this page contains elements of the officially released Method Sheet. If you require further information please refer to the full Method Sheet PDF under the given link, or contact your local Roche country representative." }, "Chapters": [ { "Name": "IntendedUse", "Value": "", "Language": "en" }, { "Name": "TestPrinciple", "Value": "", "Language": "en" }, { "Name": "MeasuringRange", "Value": "", "Language": "en" }, { "Name": "ExpectedValues", "Value": "", "Language": "en" }, { "Name": "LimitationInterference", "Value": "", "Language": "en" }, { "Name": "OrderInformation", "Value": "", "Language": "en" }, { "Name": "SystemInformation", "Value": "", "Language": "en" }, { "Name": "Handling", "Value": "", "Language": "en" }, { "Name": "TestDefinition", "Value": "", "Language": "en" }, { "Name": "StorageStability", "Value": "", "Language": "en" }, { "Name": "Calibration", "Value": "", "Language": "en" }, { "Name": "Limitations", "Value": "", "Language": "en" }, { "Name": "PerformanceData", "Value": "", "Language": "en" }, { "Name": "Precision", "Value": "", "Language": "en" }, { "Name": "MethodComparison", "Value": "", "Language": "en" }, { "Name": "Summary", "Value": "", "Language": "en" }, { "Name": "Reagents", "Value": "", "Language": "en" }, { "Name": "PrecautionsWarnings", "Value": "", "Language": "en" }, { "Name": "Caution", "Value": "", "Language": "en" }, { "Name": "QualityControl", "Value": "", "Language": "en" }, { "Name": "SpecimenPreparation", "Value": "", "Language": "en" } ] } } ] }

AMYL2

α-Amylase EPS ver.2

IVD For in vitro diagnostic use.
AMYL2

Overview

Detailed Specifications

Ordering Information

Compatible Instruments

...
    ...

    Technical Documents

    Access Material Data Sheets, Certificates of Analysis, and other product documentation.

    After clicking below, you will be redirected to eLabDoc, where you can choose your local country.
    error errorMessage
    Sorry, we couldn't find the content you are looking for
    Please try again later