Human Erythrocyte Adenosine Triphosphate D-3-Phosphoglycerate 1-Phosphotransferase*

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Abstract
Detailed procedures have been presented for the preparation of crystalline phosphoglycerate kinase from human erythrocyte. The isolation technique involved denaturation of hemoglobin with the use of ethanol-chloroform mixture followed by adsorption and elution from calcium phosphate gel, negative adsorption by diethylaminoethylcellulose, and ammonium sulfate fractionation. The purified enzyme was obtained as long-rectangular crystals. The enzyme was specific for phosphoglycerate. The turnover number was of the same order as that of the crystalline yeast enzyme. The Michaelis constants for the substrates are similar to the values of yeast and muscle enzymes reported by previous invesgators.