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Phosphorylated Vitamin D₂ and Alkaline Phosphatase Activity

Johan Throne Holst's Institute for Nutrition Research, University of Oslo, Blindern, Norway

The effect of phosphorylated vitamin D₂ (D₂P) on the activity of alkaline phosphatases which had been partially purified from intestine and bones, and a crude extract from kidney, has been investigated. Additions of D₂P to a final concentration of 5 x 10^-5 M did not affect the activity of these enzymes when the determinations were carried out under conditions for optimal enzyme activity. Various buffers have been used in these investigations. Addition of D₂P resulted in a partial reversal of the inhibitory action exerted by tetraborate on the intestinal alkaline phosphatase. Furthermore, D₂P was found to be hydrolyzed by alkaline phosphatase from the intestine. Free calciferol thus liberated will give a color with the phenol reagent of Folin and Ciocalteu.