ISOLATION AND SOME CHARACTERISTICS OF PLACENTAL ALKALINE PHOSPHATASE

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Placental alkaline phosphatase was found to be heterogeneous in respect of its gel electrophoretic migration and molecular weight. It hampered the purification of this enzyme.The present authors devised the isolation procedure to obtain this enzyme in a sufficiently pure state and in large quantity. The process included the removal of protein impurities with Japanese acid clay and carboxymethyl cellulose, and affinity chromatography on L-phenylalaninecoupled Sepharose 4 B and then on concanavalin A-labeled Sepharose 4 B.The carbohydrate content of purified enzyme preparation was as low as 6 per cent, of which major components were glucosamine and mannose. Oligosaccharide chains of this enzyme were responsible for the interaction with concanavalin A, even after exoglycosidase digestion.This enzyme possessed a-helical conformation, as documented by optical rotatory dispersion and circular dichroism measurement. This ordered conformation persisted in an alkaline solution, though it was destroyed with a simultaneous loss of activity in an acidic solution.
久留米大学医学部 The Kurume Medical Journal 編集部の論文