PLASMIN CONVERTS PRO-FORM OF GROUP-I PHOSPHOLIPASE A(2) INTO RECEPTOR-BINDING, ACTIVE FORMS

被引：27

作者：

NAKANO, T

FUJITA, H

KIKUCHI, N

ARITA, H

机构：

[1] Shionogi Research Laboratories, Shionogi and Co Ltd., Fukushima-ku, Osaka

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 198卷 / 01期

关键词：

D O I：

10.1006/bbrc.1994.1002

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：

Treatment of zymogen of pancreatic-type group I phospholipase A2 (PLA2-I) by plasmin, a fibrinolytic enzyme, increases PLA2 activity as well as receptor binding activity in a dose-and time-dependent manner. Separation of plasmin-treated pro-PLA2-I by HPLC and amino acid sequence analysis of the products revealed that, in addition to an authentic mature PLA2-I produced by trypsin, plasmin produced active products which had been modified in the C-terminal region. Thus, PLA2-I may be involved in physiologic processes which accompany the formation of plasmin. © 1994 Academic Press, Inc.

引用

页码：10 / 15

页数：6

共 27 条

[1] THROMBOXANE-A2 - ITS GENERATION AND ROLE IN PLATELET ACTIVATION [J].