STUDIES ON SWEET POTATO PHOSPHATASE

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Abstract
An en-zyme prepn. is obtained from sweet potato by fractional pptns. with 40-60% acetone and 0.40-0.65 saturation with ammonium sulfate, successively. This prepn. contains non-specific phosphatase which acts on phosphomonoester, pyrophosphate, and metaphosphate. Mutual substrate inhibition is observed only with the phenylphosphatase activity. The enzymic affinity (Km) values with [beta]-glycerophosphate and phenylphosphate are decreased by heating, while those with pyrophosphate and metaphosphate are increased. No change in the opt. pH for activity is observed by heat treatment. Starch column chromatography gives 2 fractions, both having about the similar distribution of enzymic activities, for [beta]-glycerophosphate, pyrophosphate, metaphosphate, phenylphosphate and adenosine triphosphate.