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- W1990371805 abstract "gamma-Glutamylcysteine synthetase (L-glutamate:L-cysteine gamma-ligase (ADP-forming), EC 6.3.2.2) 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." @default.
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- W1990371805 date "1980-06-01" @default.
- W1990371805 modified "2023-09-23" @default.
- W1990371805 title "Erythrocyte γ-glutamylcysteine synthetase from normal and low-glutathione sheep" @default.
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- W1990371805 doi "https://doi.org/10.1016/0005-2744(80)90109-6" @default.
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