The purification of alkaline phosphatases of animal tissues

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Abstract
The alkaline phosphatases of calf intestinal mucosa and of cow mammary gland are associated with microsomal particles. By treatment with n-butanol at 35[degree] the enzyme is readily obtained in true solution. On the basis of this effect a convenient method for assay of alkaline phosphatase of animal tissues is proposed. The purification of alkaline phosphatase from calf intestinal mucosa involves butanol treatment of washed microsomes, followed by acetone precipitation, heating and charcoal adsorption. The most active preparation had an activity (with beta-glycerophosphate) of 83,500 units/mg N(Qp 579,000). This represents a purification of over 1000 times and thus is the most active phosphatase preparation as yet obtained. The alkaline phosphatases of kidney, liver and mammary gland were partially purified by similar methods.