title: Reaction of S-nitrosoglutathione with sulfhydryl groups in protein.
abstract: The covalent modification of sulfhydryl groups by S-nitrosoglutathione has been examined using model compounds. S-Nitrosoglutathione and thiol compounds causing extremely fast transnitrosation reaction and subsequent production of mixed disulfide. Yeast alcohol dehydrogenase is rapidly inactivated by S-nitrosoglutathione. The reversibility and Ellman test demonstrate that the inactivation is the result of covalent modification of sulfhydryl groups in this enzyme.
authors.affiliation: Department of Biochemistry, Ohio State University, Columbus 43210.
authors.forename: J W
authors.initials: JW
authors.lastname: Park
mesh_terms: D000426:Alcohol Dehydrogenase; D004789:Enzyme Activation; D005978:Glutathione / Q000031:analogs & derivatives*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D009603:Nitroso Compounds; D011506:Proteins; D026422:S-Nitrosoglutathione; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012996:Solutions; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds
chemical_list: D009603:Nitroso Compounds; D011506:Proteins; D012996:Solutions; D013438:Sulfhydryl Compounds; D026422:S-Nitrosoglutathione; D000426:Alcohol Dehydrogenase; D005978:Glutathione