Effect of Zn^<2+> and Mg^<2+> on Alkaline Phosphatase from Human Placenta and Intestine

概要

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Alkaline phosphatases (orthophosphoric monoester phosphohydrolase, E.C. 3. 1. 3. 1) from human placenta and intestine are activated by Mg^<2+>, but inhibited by Zn^<2+>. In these respects, the enzymes are different from the human biliary, bone, liver and kidney enzymes, which are much activated by Mg^<2+> and Zn^<2+>. At pH 10.5,the K_m of enzymes and enzymes inhibited by inorganic phosphate are not modified by Mg^<2+>. These results suggest that the activation by Mg^<2+> proceeds through a binding of Mg^<2+> with other part of the active site of alkaline phosphatase. It was also found that the activity of alkaline phosphatases was remarkably influenced by binding metals, and Zn^<2+> and Mg^<2+> contents in both enzymes were 4 g-atoms/mole and 3-5 g-atoms/mole, respectively.
公益社団法人日本薬学会の論文
1977-04-25