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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1998-2-6
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pubmed:abstractText |
The rate of protein S-nitrosylation, a reversible process by which S-nitroso thiol (RS-NO) compounds exchange the NO+ moiety with protein SH groups, is essentially governed by two factors, the pK alpha and the accessibility of the protein sulfhydryl. A useful method of following transnitrosation kinetics of various protein and nonprotein SH compounds with GS-NO is described. When the reaction is carried out in the presence of 1-chloro-2,4-dinitrobenzene and glutathione transferases, the rate of RS-NO formation (RSH + GS-NO-->RS-NO + GSH) can be monitored by spectrophotometry at 340 nm in terms of the enzymatic conversion of GSH to a GS conjugate. Unlike methods based on NO release from the S-NO bond, this procedure is rapid and accurate and requires relatively small amounts of thiols. The second order rate constants of S-nitrosylation of human and rat oxy- and deoxyhemoglobin of BSA and other thiols were calculated by this method which confirmed previous results reported in the literature.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0003-2697
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
254
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
215-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9417779-Animals,
pubmed-meshheading:9417779-Glutathione,
pubmed-meshheading:9417779-Glutathione Transferase,
pubmed-meshheading:9417779-Hemoglobins,
pubmed-meshheading:9417779-Humans,
pubmed-meshheading:9417779-Kinetics,
pubmed-meshheading:9417779-Nitrosation,
pubmed-meshheading:9417779-Nitroso Compounds,
pubmed-meshheading:9417779-Rats,
pubmed-meshheading:9417779-Rats, Wistar,
pubmed-meshheading:9417779-Spectrophotometry
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pubmed:year |
1997
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pubmed:articleTitle |
A method to study kinetics of transnitrosation with nitrosoglutathione: reactions with hemoglobin and other thiols.
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pubmed:affiliation |
Department of Environmental Biology, University of Siena, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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