Glutathione Synthesis in Human Erythrocytes: II. PURIFICATION AND PROPERTIES OF THE ENZYMES OF GLUTATHIONE BIOSYNTHESIS

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RESUMO

The two enzymes required to synthesize glutathione de novo have been purified from human erythrocytes. Glutamylcysteine synthetase was purified 4300-fold and was approximately 80% pure based on polyacrylamide gel electrophoresis. The purified enzyme catalyzes the formation of 30.5 μmoles of γ-glutamyl-cysteine per mg of protein per hr and is inhibited by sulfhydryl inhibitors.

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