SEPARATION OF THE 2 DOMAINS OF HUMAN MUCUS PROTEINASE-INHIBITOR - INHIBITORY ACTIVITY IS ONLY LOCATED IN THE CARBOXY-TERMINAL DOMAIN

被引：17

作者：

VANSEUNINGEN, I ^{[1
]}

DAVRIL, M ^{[1
]}

机构：

[1] INSERM,U16,PL VERDUN,F-59045 LILLE,FRANCE

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 179卷 / 03期

关键词：

D O I：

10.1016/0006-291X(91)91755-2

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 mucus proteinase inhibitor is a two-domain protein which inactivates bovine trypsin and chymotrypsin, leukocyte elastase and cathepsin G. In order to localize the site(s) responsible for these inhibitory activities, the two domains were isolated after specific cleavage of the Asp49-Pro50 bond following mild acid treatment of the bronchial inhibitor. The carboxy-terminal domain was active against leukocyte elastase, trypsin and chymotrypsin whereas the amino-terminal domain, which contained a putative antitryptic active site, was devoid of activity. This implicates that, in the whole molecule, the inhibitory activity region is localized only in the carboxy-terminal domain. © 1991.

引用

页码：1587 / 1592

页数：6

共 10 条

[1]

EISENBERG SP, 1990, J BIOL CHEM, V265, P7976

[2]

FRITZ H, 1988, BIOL CHEM H-S, V369, P79

[3] THE 2.5 A X-RAY CRYSTAL-STRUCTURE OF THE ACID-STABLE PROTEINASE-INHIBITOR FROM HUMAN MUCOUS SECRETIONS ANALYZED IN ITS COMPLEX WITH BOVINE ALPHA-CHYMOTRYPSIN [J].