Hepatic alkaline phosphatase isoenzymes: isolation, characterization and differential alteration.
Although it is generally believed that hepatic alkaline phosphatase is localized to liver plasma membranes, 63% is present in the cytosol fraction after ultracentrifugation of rat liver homogenates. Divalent cation requirements, heat inactivation, pH optima, Km and chemical inhibition characteristics of partially purified alkaline phosphatase enzymes prepared from membrane and cytosol fractions suggested different structural forms. Furthermore, bile duct obstruction and ethinyl estradiol administration preferentially increased membrane-bound alkaline phosphatase activity, while cytosol activity was unaltered. In contrast, phenobarbital treatment decreased membrane-bound alkaline phosphatase and increased cytosol activity. These studies support the presence of two forms of hepatic alkaline phosphatase in rat liver which are regulated by different control mechanisms.
D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism; D000818:Animals; D002413:Cations, Divalent; D004492:Edetic Acid / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
D002413:Cations, Divalent; D007527:Isoenzymes; D004492:Edetic Acid; D000469:Alkaline Phosphatase; D008274:Magnesium