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The enolase of the human erythrocyte


, : The enolase of the human erythrocyte. Canadian Jour Biochem And Physiol 40(8): 1005-1018

The enolase activity of the human erythrocyte has been studied with a partially purified preparation of the enzyme. The enzyme was found to have an absolute requirement for Mg 2+ ions. A kinetic study of the influence of the concentration of Mg ions and 2-phosphoglycerate on the formation of phosphoenolpyruvate from 2-phosphoglycerate has shown that the active complex of enzyme, substrate, and activator (Mg2+) can be formed in several ways. With low concentrations of substrate and Mg2+ the reaction was maximum at pH 7.0; with high concentrations of both, the activity was maximum over a wide range of hydrogen ion concentrations on the acid side of neutrality (at least from pH 6.3 to 7.0) and decreased above pH 7.0.

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