Phosphorylated Vitamin D2 and Alkaline Phosphatase Activity

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Abstract
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 × 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.