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Glutathione Synthesis in Human Erythrocytes: II. PURIFICATION AND PROPERTIES OF THE ENZYMES OF GLUTATHIONE BIOSYNTHESIS
Philip W. Majerus, M. J. Brauner, M. B. Smith, Virginia Minnich
Philip W. Majerus, M. J. Brauner, M. B. Smith, Virginia Minnich
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Glutathione Synthesis in Human Erythrocytes: II. PURIFICATION AND PROPERTIES OF THE ENZYMES OF GLUTATHIONE BIOSYNTHESIS

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Abstract

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.

Authors

Philip W. Majerus, M. J. Brauner, M. B. Smith, Virginia Minnich

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