| pubmed-article:9917330 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9917330 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:9917330 | lifeskim:mentions | umls-concept:C0017817 | lld:lifeskim |
| pubmed-article:9917330 | lifeskim:mentions | umls-concept:C0038734 | lld:lifeskim |
| pubmed-article:9917330 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9917330 | pubmed:dateCreated | 1999-2-22 | lld:pubmed |
| pubmed-article:9917330 | pubmed:abstractText | The modification of reactive protein sulfhydryls by S-nitrosoglutathione and other NO donors has been studied by gel isoelectric focusing. S-nitrosylated, unmodified, and S-glutathiolated protein forms are differentiated by this method. With specific antibodies for the protein of interest, both S-nitrosylation and S-glutathiolation of the protein were analyzed in mixtures obtained as soluble tissue or cell extracts. The effect of S-nitrosoglutathione (GSNO) on purified phosphorylase b, on carbonic anhydrase III in an extract from rat liver, and on H-ras expressed in Escherichia coli was examined. When fresh GSNO reacted with pure phosphorylase b, only S-nitrosylated forms of the protein were observed. Likewise the NO donors, amyl nitrite, spermine NONOate, and diethylamine NONOate, all generated S-nitrosylated phosphorylase b. When crude mixtures of proteins from rat liver (containing carbonic anhydrase III) or from E. coli (containing an overexpressed form of H-ras) were exposed to fresh GSNO, both the S-nitrosylated and the S-glutathiolated forms of the proteins were observed. It is suggested that reactive intermediates from the breakdown of GSNO are responsible for the observed S-glutathiolation. These experiments show that both S-nitrosylated and S-glutathiolated forms of proteins may be generated by the addition of GSNO to mixtures containing proteins with reactive sulfhydryls. These protein modifications may exhibit metabolic consequences independent of the release of nitric oxide. | lld:pubmed |
| pubmed-article:9917330 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9917330 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9917330 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9917330 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9917330 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9917330 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:9917330 | pubmed:author | pubmed-author:ThomasJ AJA | lld:pubmed |
| pubmed-article:9917330 | pubmed:author | pubmed-author:SiewDD | lld:pubmed |
| pubmed-article:9917330 | pubmed:author | pubmed-author:AkerboomT PTP | lld:pubmed |
| pubmed-article:9917330 | pubmed:author | pubmed-author:JOCC | lld:pubmed |
| pubmed-article:9917330 | pubmed:copyrightInfo | Copyright 1999 Academic Press. | lld:pubmed |
| pubmed-article:9917330 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9917330 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9917330 | pubmed:volume | 362 | lld:pubmed |
| pubmed-article:9917330 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9917330 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9917330 | pubmed:pagination | 67-78 | lld:pubmed |
| pubmed-article:9917330 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9917330 | pubmed:meshHeading | pubmed-meshheading:9917330-... | lld:pubmed |
| pubmed-article:9917330 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:9917330 | pubmed:articleTitle | S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione. | lld:pubmed |
| pubmed-article:9917330 | pubmed:affiliation | Department of Biochemistry, Iowa State University, Ames, Iowa, 50011, USA. | lld:pubmed |
| pubmed-article:9917330 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9917330 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:9917330 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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