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  • Title: A membrane-bound phospholipase C with an apparent specificity for lysophosphatidylinositol in porcine platelets.
    Author: Murase S, Okuyama H.
    Journal: J Biol Chem; 1985 Jan 10; 260(1):262-5. PubMed ID: 3917432.
    Abstract:
    A membrane preparation from porcine platelets catalyzed the hydrolysis of [2-3H]glycerol-labeled lysophosphatidylinositol to form monoacylglycerol and inositol phosphates. The hydrolysis was optimal at pH 9. The addition of Ca2+ did not enhance the hydrolysis, but the enzyme was inhibited completely by EGTA. The EGTA-inactivated enzyme was partially reactivated by Ca2+; Mn2+, Mg2+, and Zn2+ were much less effective or ineffective for the reactivation. The phospholipase C was apparently specific for lysophosphatidylinositol; phosphatidylinositol, phosphatidylcholine, phosphatidylethanolamine, lysophosphatidylcholine, lysophosphatidylethanolamine, phosphatidic acid, and lysophosphatidic acid were not hydrolyzed at significant rates under the conditions used. Phospholipase C with these properties has not been reported previously.
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