title: [Determination of the esterase activity of serine proteinases using synthetic substrates].
abstract: The authors suggest a highly sensitive rapid and simple method for measuring esterase activities of bovine pancreatic chymotrypsin, human neutrophilic cathepsin D, and elastase, and of human blood serum chymotrypsin-like esterase and elastase-like esterase activities, with fluorogenic synthetic ethers, amino acid derivatives, employed as substrates: N-benzoxycarbonylphenylalanine 4-methylumbelliferyl ester (Z-Phe-OMC) and tret-butyloxycarbonyl-1-alanine 4-methylumbelliferyl ester (BOC-Ala-OMC).
authors.forename: L N
authors.initials: LN
authors.lastname: Kraeva
authors.forename: V F
authors.initials: VF
authors.lastname: Pozdnev
authors.forename: V N
authors.initials: VN
authors.lastname: Kokriakov
authors.forename: A A
authors.initials: AA
authors.lastname: Usova
mesh_terms: D000818:Animals; D002417:Cattle; D004950:Esterases / Q000378:metabolism*; D006801:Humans; D006923:Hymecromone / Q000031:analogs & derivatives; D012697:Serine Endopeptidases / Q000378:metabolism*
chemical_list: C070487:tert-butyloxycarbonyl-1-alanine 4-methylumbelliferyl ester; D006923:Hymecromone; C047960:benzyloxycarbonylphenylalanine 4-methylcoumaryl-7-ester; D004950:Esterases; D012697:Serine Endopeptidases
vernacular_title: Opredelenie ésteraznoĭ aktivnosti serinovykh proteinaz s ispol'zovaniem sinteticheskikh substratov.