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- W1593769894 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." @default.
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- W1593769894 date "1985-01-01" @default.
- W1593769894 modified "2023-09-30" @default.
- W1593769894 title "A membrane-bound phospholipase C with an apparent specificity for lysophosphatidylinositol in porcine platelets." @default.
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- W1593769894 doi "https://doi.org/10.1016/s0021-9258(18)89725-3" @default.
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