Abstract
Synthesized 1-(3H)-linoleoyl-2-(14C) linoleoyl glycerophosphoryl choline (PC) served as substrate for postheparin human plasma phospholipase activity. Essentially, no enzymatic activity could be found in pre-heparin plasma. Following i.v. heparin injection, however, the time course of phospholipase activity coincided with triglyceride lipase, diglyceride hydrolase and monoglyceride hydrolase activity which have been demonstrated in post-heparin plasma before. With double labelled PC it could be shown that there was no absolute positional specificity for either the α1 or β position in the lecithin molecule, but both fatty acid moieties are hydrolyzed with post-heparin plasma. This may be due to one single phospholipase or two separate phospholipases A1 and A2. Both enzymatic activities were found to be normal in patients with familial hyperlipoproteinemia type I (genetic deficiency of post-heparin plasma triglyceride lipase), type II, type III and type IV.
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