MODULATION OF PURIFIED PHOSPHOLIPASE-A2 ACTIVITY FROM HUMAN-PLATELETS BY CALCIUM AND INDOMETHACIN

被引：151

作者：

JESSE, RL

FRANSON, RC

机构：

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 575卷 / 03期

基金：

美国国家卫生研究院;

关键词：

(Human platelets); Ca[!sup]2+[!/sup; Indomethacin; Phospholipase A[!sub]2[!/sub;

D O I：

10.1016/0005-2760(79)90117-6

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 membrane bound phospholipase A2 (phosphatide 2-acylhydrolase, EC 3.1.1.4) from human platelets has been purified 3500-fold, and partially characterized. Phospholipase A2 activity was assayed using [1-14C] oleate-labeled Escherichia coli or sonicated dispersions of synthetic phospholipids. The 2-acyl specificity of the phospholipase activity was confirmed using phosphatidylethanolamine labeled in the C-1 position as substrate. The purified enzyme was maximally active between pH 8.0 and 10.5, and had an absolute requirement for low concentrations of Ca2+ Indomethacin, but not aspirin, inhibited phospholipase A2 activity. © 1979.

引用

页码：467 / 470

页数：4

共 11 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] PHOSPHOLIPASE-A AND ITS ZYMOGEN FROM PORCINE PANCREAS .3. ACTION OF ENZYME ON SHORT-CHAIN LECITHINS [J].