PMID: 42441Dec 18, 1979

Modulation of purified phospholipase A2 activity from human platelets by calcium and indomethacin

Biochimica Et Biophysica Acta
R L Jesse, R C Franson

Abstract

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(-14)C] 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.

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Related Concepts

Blood Platelets
Calcium
Hydrogen-Ion Concentration
Osmosin
Phospholipase
Phospholipases A
Phospholipases A2

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