Abstract
A membrane bound phospholipase A 2 (phosphatide 2-acylhydrolase, EC 3.1.1.4) from human platelets has been purified 3500-fold, and partially characterized. Phospholipase A 2 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 Ca 2+ Indomethacin, but not aspirin, inhibited phospholipase A 2 activity.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
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