PMID: 6108786Jun 13, 1980Paper

Erythrocyte gamma-glutamylcysteine synthetase from normal and low-glutathione sheep

Biochimica Et Biophysica Acta
P G BoardD Ou


gamma-Glutamylcysteine synthetase (L-glutamate:L-cysteine gamma-ligase (ADP-forming), EC was purified from the erythrocytes of normal and low-glutathione sheep. The molecular weight (78 000), pH optimum (pH 7), substrate specificity, inhibition constant for glutathione (0.44-0.50 mM), electrophoretic mobility, and heat stability were similar for the purified enzyme from both sources. Using immunological techniques, the specific activity of gamma-glutamylcysteine synthetase from low-glutathione sheep was lower than that from normal sheep.


Apr 6, 1973·Science·A Meister
Jan 1, 1974·Acta Obstetricia Et Gynecologica Scandinavica·K B Hansen
Oct 20, 1967·Science·J E Smith, B I Osburn

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Oct 1, 1983·Biochemical Genetics·E M TuckerJ D Young
Nov 6, 1989·Biochimica Et Biophysica Acta·T OginoM Awai
Sep 1, 1984·Analytical Biochemistry·G F Seelig, A Meister
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