Zobrazeno 1 - 10
of 449
pro vyhledávání: '"Alton Meister"'
Autor:
Alton Meister
Publikováno v:
Nutrition Reviews. 42:397-410
Autor:
Alton Meister
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1271:35-42
Glutathione deficiency produced by giving buthionine sulfoximine (an inhibitor of gamma-glutamylcysteine synthetase) to animals, leads to biphasic decline in cellular glutathione levels associated with sequestration of glutathione in mitochondria. Li
Publikováno v:
Journal of Biological Chemistry. 270:12471-12475
Mutant human γ-glutamyl transpeptidases with amino acid substitutions on the light subunit at the Asp residues conserved among several species, and at the unique cysteine residue (Cys-454), were prepared and expressed in a baculovirus insect cell sy
Autor:
Terry K. Smith, Alton Meister
Publikováno v:
Journal of Biological Chemistry. 270:12476-12480
γ-Glutamyl transpeptidase, an enzyme of central significance in glutathione metabolism, is inactivated by iodoacetamide, which esterifies an active site carboxyl group identified here as that of Asp-422. Treatment of the inactivated enzyme with hydr
Publikováno v:
Proceedings of the National Academy of Sciences. 92:2360-2364
Acivicin is a potent inhibitor of gamma-glutamyl transpeptidase (EC 2.3.2.2), an enzyme of importance in glutathione metabolism. Acivicin inhibition and binding are prevented by gamma-glutamyl substrates and analogs (e.g., serine plus borate), consis
Publikováno v:
Proceedings of the National Academy of Sciences. 92:1232-1236
Glutathione (GSH) synthetase [gamma-L-glutamyl-L-cysteine:glycine ligase (ADP-forming), EC 6.3.2.3], an enzyme present in almost all cells, catalyzes the ATP-dependent synthesis of GSH from gamma-L-glutamyl-L-cysteine and glycine. Highly purified pre
Publikováno v:
Proceedings of the National Academy of Sciences. 92:126-130
A mutant of human gamma-glutamyl transpeptidase (EC 2.3.2.2, a membrane-bound enzyme of importance in glutathione metabolism) that differs from the wild type by deletion of the putative signal peptide/anchor domain (amino acid residues 1-27) was expr
Publikováno v:
Journal of Biological Chemistry. 269:21435-21439
Inactivation of gamma-glutamyl transpeptidase by acivicin (L-(alpha S,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazole acetic acid) is rapid, thought to be irreversible, and associated with binding of close to 1 mol of inhibitor/mol of enzyme. Previo
Autor:
Alton Meister
Publikováno v:
Journal of Biological Chemistry. 269:9397-9400
strong evolutionary link between GSH and eukaryotic aerobic metabolism that is reflected in the function of GSH in protection against oxygen toxicity (2). GSH is not required in the diet of animals but is synthesized in virtually all animal cells' by
Publikováno v:
Circulation Research. 74:115-120
Results from in vitro experiments suggest that development of nitrate tolerance is due to a depletion of vascular thiol compounds (ie, cysteine and glutathione [GSH]) necessary for the bioconversion of organic nitrates. However, it is unknown whether