Prostataphosphatase. 2. Mitteilung.

Abstract
Prostate phosphatase is most stable at pH 4 to 6. It hydrolyzes [beta]-glyeerophosphate most rapidly at pH 5.4. The optimum glycerophosphate concentration is 0.15 M. The enzyme is not influenced by the presence of Mg or cystein. It is inhibited by NaF. Alcohols irreversibly inactivate it. The enzyme is best purified by electro-dialysis of chopped gland autolysate. Protein impurities are precipitated, leaving a preparation capable of liberating up to 3/4 its own weight of H3PO4 per second.

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