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  • Title: Bicarbonate-stimulated ATPase activity of bovine liver alkaline phosphatase.
    Author: Corbic M, de Couët G, Bertrand O, Cochet S, Erlinger S.
    Journal: J Hepatol; 1985; 1(2):167-78. PubMed ID: 2414359.
    Abstract:
    A commercial preparation of bovine hepatic alkaline phosphatase was found to have a Mg2+-stimulated ATPase activity. The pH optimum was 8.5, the Km for ATP was 4.2 X 10(-5) M and the Vmax was 88.3 mumol Pi . h-1 . mg-1. HCO3- had a stimulatory effect on Mg2+ -ATPase activity. Other anions had no effect or an inhibitory effect while Na+, K+ and ouabain had no effect. Purification of the commercial preparation by gel filtration and affinity chromatography yielded a fraction with alkaline phosphatase and (Mg2+ + HCO3-)ATPase activities that had been enriched respectively 27-fold and 23-fold; both activities were inhibited by levamisole (93.1% and 93.8%, respectively) and the purified fraction was found to be a single protein on sodium dodecyl sulfate polyacrylamide gel electrophoresis. These results suggest that alkaline phosphatase and (Mg2+ + HCO3-)ATPase may be properties of the same liver protein that might be involved in biliary HCO3- transport and bile secretion.
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