INACTIVATION OF HUMAN ALPHA1 PROTEINASE-INHIBITOR BY THIOL PROTEINASES

被引：124

作者：

JOHNSON, D

TRAVIS, J

机构：

[1] UNIV GEORGIA, DEPT BIOCHEM, ATHENS, GA 30602 USA

[2] STRANGEWAYS RES LAB, DEPT TISSUE PHYSIOL, CAMBRIDGE CB1 4RN, ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1977年 / 163卷 / 03期

关键词：

D O I：

10.1042/bj1630639

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 .alpha.1 proteinase inhibitor is the body''s principal modulator of serine proteinases (such as those released from phagocytic cells). Cysteine-active-site proteinases, which are not inhibited, inactivate this important inhibitor by proteolytic cleavage of a scissile peptide bond. Papain carries out this inactivation catalytically, whereas human liver cathepsin B1 acts stoicheiometrically. Thus thiol proteinases could easily disrupt the delicately regulated balance between serine proteinases and .alpha.1 proteinase inhibitor.

引用

页码：639 / +

页数：1

共 17 条

[1] HUMAN CATHEPSIN-B1 - PURIFICATION AND SOME PROPERTIES OF ENZYME [J].