Add time:09/05/2019         Source:sciencedirect.com

A phosphatase preparation has been partially purified from beef brain which catalyzes the hydrolysis of phosphohydroxypyruvic acid, β-glycerophosphate, glucose-6-phosphate, and fructose-6-phosphate. The pH optimum for the first two substrates is in the range of 7.5. Magnesium ions are required for optimal activity, and the reaction is inhibited by fluoride and manganese. The enzyme preparation has negligible activity with phosphoserine, p-nitrophenylphosphate, 5′-mononucleotides, 3-phosphoglycerate, and phosphoethanolamine. The Km values for phosphohydroxypyruvate and dl-β-glycerophosphate are 7 × 10−3M and 6 × 10−4M, respectively.

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