COMPARATIVE STUDIES ON HUMAN CARBOXYPEPTIDASE-B AND CARBOXYPEPTIDASE-N

被引：58

作者：

MCKAY, TJ ^{[1
]}

PHELAN, AW ^{[1
]}

PLUMMER, TH ^{[1
]}

机构：

[1] NEW YORK STATE DEPT HLTH,DIV LABS & RES,ALBANY,NY 12201

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 1979年 / 197卷 / 02期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/0003-9861(79)90271-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 × 10-6 m for Carboxypeptidases B and N, respectively. Values for the all-carbon guanidinopropylsuccinic acid were similar. In addition the kinetic parameters, Km and kcat Km, 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. © 1979.

引用

页码：487 / 492

页数：6

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