| pubmed-article:8651684 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C0038838 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C0596040 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C0439807 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C0136157 | lld:lifeskim |
| pubmed-article:8651684 | lifeskim:mentions | umls-concept:C1176299 | lld:lifeskim |
| pubmed-article:8651684 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8651684 | pubmed:dateCreated | 1996-7-22 | lld:pubmed |
| pubmed-article:8651684 | pubmed:abstractText | We have reexamined the formation and reactions of radicals formed from peroxynitrite (ONOO-)-mediated oxidation of glutathione (GSH), L-cysteine (Cys), N-acetyl-D,L-penicillamine (NAP), and sodium bisulfite (NaHSO3). Sulfur-centered and superoxide union radicals were trapped using 5,5-dimethyl-1-pyrroline-N-oxide (DMPO) and the radical adducts were analyzed by electron spin resonance (ESR) spectroscopy. The following sulfur-centered radicals were detected: glutathionyl radical (GS') from GSH, L-cysteinyl radical ('Scys) from L-cysteine, N-acetyl-D,L-penicillamine thiyl radical ('SNAP) from NAP, and sulfite anion radical (SO3-.) from NaHSO3. Additionally the formation of the hydroxyl radical adduct of DMPO (DMPO/'OH) was observed. DMPO/'OH formation was totally inhibited by low-molecular-weight superoxide dismutase (SOD) mimics. This suggests that DMPO/'OH was formed from the decay of the superoxide radical adduct of DMPO. In the presence of SOD mimics, the DMPO-sulfur-centered adducts were more persistent, suggesting that O2-. is partially responsible for the instability of DMPO-thiyl adducts. Sulfur-centered radicals formed during oxidation of thiols and sulfite by peroxynitrite react with ammonium formate to form the carbon dioxide anion radical (CO2-.). We conclude that sulfur-centered radicals produced from the oxidation of thiols and sulfite by peroxynitrite arise from a hydroxyl-radical-independent mechanism. Biological implications of peroxynitrite-mediated oxidation of thiols as well as the use of SOD mimics in biological spin-trapping are discussed. | lld:pubmed |
| pubmed-article:8651684 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8651684 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8651684 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8651684 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8651684 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8651684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8651684 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8651684 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8651684 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8651684 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:8651684 | pubmed:author | pubmed-author:KalyanaramanB... | lld:pubmed |
| pubmed-article:8651684 | pubmed:author | pubmed-author:HoggNN | lld:pubmed |
| pubmed-article:8651684 | pubmed:author | pubmed-author:KarouiHH | lld:pubmed |
| pubmed-article:8651684 | pubmed:author | pubmed-author:JosephJJ | lld:pubmed |
| pubmed-article:8651684 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8651684 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8651684 | pubmed:volume | 330 | lld:pubmed |
| pubmed-article:8651684 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8651684 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8651684 | pubmed:pagination | 115-24 | lld:pubmed |
| pubmed-article:8651684 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8651684 | pubmed:meshHeading | pubmed-meshheading:8651684-... | lld:pubmed |
| pubmed-article:8651684 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8651684 | pubmed:articleTitle | Effect of superoxide dismutase mimics on radical adduct formation during the reaction between peroxynitrite and thiols--an ESR-spin trapping study. | lld:pubmed |
| pubmed-article:8651684 | pubmed:affiliation | Biophysics Research Institute, Medical College of Wisconsin, Milwaukee 53226, USA. | lld:pubmed |
| pubmed-article:8651684 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8651684 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8651684 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8651684 | lld:pubmed |
