Properties of alkaline-phosphatase fractions separated by starch-gel electrophoresis

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Abstract
Starch-gel electrophoresis of concentrated butan-1-ol extracts of human bone, liver, kidney and small intestine reveals a number of active alkaline-phosphatase tractions in each. The apparent Km values (substrate, B-naphthyl phosphate) of the individual enzyme bands from these tissues have been determined. Other properties of the bands, namely pH optimum, activation by Mg2+ ions and inactivation by heating at 55[degree] and pH 7, have also been studied. The phosphatase fractions from a given organ are similar in these properties and in Km values although there are some differences between phosphatases from different tissues. The significance of these findings is discussed.