Tetrameric alkaline phosphatase in human liver plasma membranes.
Molecular weights of native membrane-bound alkaline phosphatase released by butanol and by nonionic detergents were more than twice that of the purified dimeric enzyme. Alkaline phosphatase released by phosphatidylinositol-specific phospholipase-C was of both high and low molecular weight: the former was a protomer of a single protein of the same molecular size as monomeric alkaline phosphatase. We conclude that the membrane-bound enzyme is probably a tetramer.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000440:Butanols / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D002845:Chromatography; D003902:Detergents; D004355:Drug Stability; D006801:Humans; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D012995:Solubility; D010738:Type C Phospholipases / Q000378:metabolism
D000440:Butanols; D003902:Detergents; D046911:Macromolecular Substances; D000469:Alkaline Phosphatase; D010738:Type C Phospholipases