Effect of phospholipase C on high-molecular-mass alkaline phosphatase in serum.
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.
D000328:Adult; D000368:Aged; D000469:Alkaline Phosphatase / Q000097:blood*; D001842:Bone and Bones / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007527:Isoenzymes / Q000032:analysis; D008099:Liver / Q000201:enzymology; D008875:Middle Aged; D008970:Molecular Weight; D010738:Type C Phospholipases / Q000494:pharmacology*
D007527:Isoenzymes; D000469:Alkaline Phosphatase; D010738:Type C Phospholipases