Abstract
Alkaline phosphatase (EC 3.1.3.1) from cow's milk has been prepared (purification ratio: 7440 times) from buttermilk by means of the following techniques; n-butanol extraction, ammonium sulfate precipitation, Sephadex G-200 filtration and ion-exchange chromatography on DEAE-cellulose columns. Upon ultracentrifugation, electrophoresis and Sephadex G-200 filtration the above preparation appeared homogeneous. The molecular weight has been measured by means of analytical filtration on a Dextran column (190 000) and by means of ultracentrifugation (160 000–170 000). The sedimentation constant s and the diffusion coefficient D were 6.0 S and 3.4 · 10 −7 cm 2/s. The amino acid composition of the purified enzyme has been determined. The stereospecific effect of l-phenylalanine on the enzyme was low and of the uncompetitive type.
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