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  • Title: [Determination of esterase activity of human and animal serine proteinases using fluorogenic esters of amino acids as substrates].
    Author: Kraeva LN, Kokriakov VN, Pozdnev VF, Morozov VI, Usova AA.
    Journal: Biull Eksp Biol Med; 1992 Jun; 113(6):600-1. PubMed ID: 1446026.
    Abstract:
    Two fluorogenic derivatives of amino acids are proposed as substrates for the purpose of enzymatic assay: N-benzyloxycarbonyl-phenylalanine-4-methyl umbelliferyl ester (substrate-1) and tert-butyloxycarbonyl-alanine-4-methyl-umbelliferyl ester (substrate-II). Chymotrypsin-like (hydrolysis of substrate-1), elastase-like (hydrolysis of substrate-II) esterase activity of bovine pancreatic chymotrypsin, activities of cathepsin G and elastase from human, porcine and rat neutrophils and esterase activity of human, porcine and rat serum were assayed. Differences in the level of chymotrypsin-like and elastase-like activities of human, porcine and rat serum were established. Activities of purified elastase and cathepsin G from human and animal neutrophils were shown to have no significant distinctions.
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