Purification and properties of alkaline phosphatase from human bile.

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Abstract
Human biliary alkaline phosphatase was purified by butanol treatment, protamine sulfate treatment, diethylaminoethyl (DEAE)-cellulose, carboxymethyl (CM)-cellulose, Sephadex G-200 and DEAE-Sephadex A-50. The purified enzyme exhibited a single protein band by disc electrophoresis. It was found that the properties of the purified biliary alkaline phosphatase was similar to those of human placental and intestinal alkaline phosphatases in relation to the influence of chemicals, optimum pH, pH stability and isoelectric point but the biliary enzyme was less stable against heat than the placental enzyme.

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