Abstract
Summary
Many of the properties of the so-called postheparin plasma phospholipase were found to be similar to those of postheparin plasma lipase. Dissimilarities were mainly in the effects of various cations, suggesting that the differences observed were due to the electrolytic effects on the substrate micelles rather than differences in enzyme species. The site of attack by postheparin plasma on the α'-C of the phospholipid molecule was confirmed with synthetic phospholipids. The similar properties of the two enzymic activities and the inability to separate the two enzyme species physically suggest that a single enzyme is capable of hydrolyzing both glyceride and phospholipid molecules. That this enzyme is a lipase and not a phospholipase is indicated by the preferential attack on the α'-C of the phospholipid molecule and by the heat lability of the enzyme.
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