KINETIC STUDY OF INHIBITION OF HUMAN AND BOVINE TRYPSINS AND CHYMOTRYPSINS BY INTER-ALPHA-INHIBITOR FROM HUMAN-PLASMA

被引：43

作者：

AUBRY, M ^{[1
]}

BIETH, J ^{[1
]}

机构：

[1] UNIV LOUIS PASTEUR, UER SCI PHARM, CHIM BIOL LAB, F-67083 STRASBOURG, FRANCE

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1976年 / 438卷 / 01期

关键词：

D O I：

10.1016/0005-2744(76)90238-2

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：

Human plasma inter-.alpha.-inhibitor forms 1:1 inactive complexes with human and bovine trypsins (EC 3.4.21.4) and chymotrypsins (EC 3.4.21.1). The association and dissociation rate constants as well as the equilibrium dissociation constants (Ki) of the complexes formed of inter-.alpha.-inhibitor and the 4 proteases were measured. The most stable complexes are those formed with the bovine enzymes. For instance, Ki = 2.1 .cntdot. 10-11 M for bovine trypsin whereas Ki = 1.2 .cntdot. 10-3 M for human trypsin. Whatever the species, the complexes formed with the chymotrypsins are less stable than those formed with the trypsins.

引用

页码：221 / 230

页数：10

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