| Human glutathione transferase catalysis of the formation of S-nitrosoglutathione from organic nitrites plus glutathione. | |
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MedLine Citation:
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PMID: 8082808 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The kinetics of spontaneous and human glutathione transferase catalysed formation of S-nitrosoglutathione (GSNO) from glutathione (GSH) and n-butyl- or amyl nitrite have been studied. At physiological pH and temperature, k2 values of 22.3 and 21.0 M-1.min-1 were obtained for n-butyl- and amyl nitrites, respectively. Rate enhancements, (kcat/Km x k2) x 10(-4), due to purified human GSH transferases A1-1, A2-2 and M1a-1a were, respectively, 7.00, 2.94 and 10.6 for n-butyl nitrite and 121, 3.92 and 34.5 for amyl nitrite. GSH transferase P1-1 showed no detectable catalysis of the formation of GSNO. The data suggest that the presence of GSTs A1-1, A2-2 or M1-1 contribute substantially to intracellular metabolism of alkyl nitrites to GSNO. The results may be significant with regard to the immunotoxicity of alkyl nitrites. |
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Authors:
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D J Meyer; H Kramer; B Ketterer |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: FEBS letters Volume: 351 ISSN: 0014-5793 ISO Abbreviation: FEBS Lett. Publication Date: 1994 Sep |
Date Detail:
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Created Date: 1994-10-13 Completed Date: 1994-10-13 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0155157 Medline TA: FEBS Lett Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 427-8 Citation Subset: IM |
Affiliation:
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Department of Biochemistry and Molecular Biology, University College London, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Catalysis Glutathione / analogs & derivatives*, metabolism* Glutathione Transferase / metabolism* Humans Kidney / enzymology Liver / enzymology Nitrites / metabolism* Nitroso Compounds / metabolism* S-Nitrosoglutathione |
| Chemical | |
Reg. No./Substance:
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0/Nitrites; 0/Nitroso Compounds; 57564-91-7/S-Nitrosoglutathione; 70-18-8/Glutathione; EC 2.5.1.18/Glutathione Transferase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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