Purification of acid phosphomonoesterase from Phaseolus mungo seedlings is reported here. Phosphatase homogeneity was evaluated at 85—90% by several methods. The enzyme is a single polypeptide chain of molecular weight 55000 ± 5000 daltons with serine and leucine as the N and C terminal residues, respectively. A saccharidic fraction containing 8% of protein weight as reducing sugar and 3% as amino sugars was found. Attempts to dissociate the saccharidic and protein moieties were unsuccessful. It was concluded that a single phosphatase was active toward phosphomonoesters, phosphoanhydride, and β‐D‐glycosyl 1‐phosphate.
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