Electrophoretic characterization of hepatic alkaline phosphatase released by phosphatidylinositol-specific phospholipase C. A comparison with liver membrane and serum-soluble forms

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Abstract
Alkaline phosphatase was solubilized from plasma membrane of rat liver and butan-l-ol, bile acids or sodium deoxycholate and electrophoretically compared with a soluble form in serum which was derived from the liver. The 3 enzyme preparations from the plasma membrane migrated at the same position on polyacrylamide-gel electrophoresis [PAGE] in the presence of either Triton X-100 or sodium dodecyl sulfate. The mobility of them, was distinctly different from that of the serum-soluble form of the liver-derived alkaline phosphatase. Phosphatidylinositol-specific phospholipase C isolated from Bacillus cereus was used to release alkaline phosphatase from plasma membrane. The released alkaline phosphatase was demonstrated to have the same mobility as the serum-soluble form on PAGE in the presence or absence of detergents. The phospholipase C also converted the butan-1-ol-extracted membrane form into the serum-soluble form. Release of alkaline phosphatase from the liver into serum is not simply caused by a detergent effect of bile salts, but involves an enzymic hydrolysis of phosphatidylinositol, with which alkaline phosphatase may strongly interact in the membrane.

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