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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1985-3-11
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pubmed:abstractText |
Protein mixed-disulfides in cultured rat heart cells were analyzed by gel electrophoresis under conditions that eliminated artifactual formation of these protein derivatives. Protein S-thiolation (protein mixed-disulfide formation) was detectable under normal culture conditions. Diamide oxidized intracellular glutathione in these cells and produced extensive protein S-thiolation. The specificity of this protein modification indicates a role in the regulation of cardiac metabolism.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
844
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
50-4
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3967051-Animals,
pubmed-meshheading:3967051-Azo Compounds,
pubmed-meshheading:3967051-Cystine,
pubmed-meshheading:3967051-Diamide,
pubmed-meshheading:3967051-Disulfides,
pubmed-meshheading:3967051-Glutathione,
pubmed-meshheading:3967051-Molecular Weight,
pubmed-meshheading:3967051-Muscle Proteins,
pubmed-meshheading:3967051-Myocardium,
pubmed-meshheading:3967051-Oxidation-Reduction,
pubmed-meshheading:3967051-Rats
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pubmed:year |
1985
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pubmed:articleTitle |
Protein mixed-disulfides in cardiac cells. S-thiolation of soluble proteins in response to diamide.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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