Erythrocyte gamma-glutamylcysteine synthetase from normal and low-glutathione sheep.
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.
D000818:Animals; D004912:Erythrocytes / Q000201:enzymology*; D005721:Glutamate-Cysteine Ligase / Q000097:blood*; D005978:Glutathione / Q000172:deficiency* / Q000494:pharmacology; D007120:Immunochemistry; D008970:Molecular Weight; D010453:Peptide Synthases / Q000097:blood*; D012756:Sheep / Q000097:blood*
D010453:Peptide Synthases; D005721:Glutamate-Cysteine Ligase; D005978:Glutathione