Clinical Chemistry
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Clinical Chemistry 32: 1503-1505, 1986;
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Clinical Chemistry, Vol 32, 1503-1505, Copyright © 1986 by American Association for Clinical Chemistry

Effect of phospholipase C on high-molecular-mass alkaline phosphatase in serum

E Sykes, FL Kiechle and E Epstein

Electrophoresis of some serum samples on polyacrylamide gel, followed by staining for alkaline phosphatase (EC 3.1.3.1), produces a band of activity at the gel origin. This high-Mr band consists of liver membrane fragments containing alkaline phosphatase and other enzymes. Alkaline phosphatase is closely associated with phosphatidylinositol in liver plasma membranes, and we have found that phospholipase C (EC 3.1.4.3) from Bacillus cereus, known to possess some phosphatidylinositol specificity, was able to release liver alkaline phosphatase from the high-Mr band. Two preparations of phospholipase C from Clostridium perfringens, however, which has no phosphatidylinositol specificity, had no effect on the alkaline phosphatase activity in the high-Mr band.




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Copyright © 1986 by the American Association for Clinical Chemistry.