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Comparative studies on human carboxypeptidases B and N
Authors:T J McKay  A W Phelan  T H Plummer
Institution:Division of Laboratories and Research, New York State Department of Health, Albany, New York, 12201 U.S.A.
Abstract:A series of dicarboxylic acid bi-product analogs of lysine and arginine have been tested as competitive inhibitors of human pancreatic carboxypeptidase B and human plasma carboxypeptidase N. The most effective derivative was guanidinoethylmercaptosuccinic acid with Kis of 0.5 and 1.0 × 10?6m for Carboxypeptidases B and N, respectively. Values for the all-carbon guanidinopropylsuccinic acid were similar. In addition the kinetic parameters, Km and kcatKm, have been determined for the hydrolysis of benzoyl-alanyl-lysine and benzoylalanyl-arginine by human Carboxypeptidases B and N. These substrates have been proposed for use in improved spectrophotometric assays. An enhanced affinity of these substrates versus benzoyl-glycyl-lysine or benzoyl-glycyl-arginine indicates a significant participation of the penultimate amino acid in catalysis of substrate.
Keywords:To whom all correspondence should be directed  
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