Source:http://linkedlifedata.com/resource/pubmed/id/18078330
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-1-3
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pubmed:abstractText |
Sulfenic acid is formed upon oxidation of thiols and is a central intermediate in the redox modulation of an increasing number of proteins. Methods for quantifying or even detecting sulfenic acid are scarce. Herein, the reagent 7-chloro-4-nitrobenz-2-oxa-1,3-diazole was determined not to be suitable as a chromophoric probe for sulfenic acid in human serum albumin (HSA-SOH) because of lack of specificity. Thionitrobenzoate (TNB) reacted with HSA exposed to hydrogen peroxide, but not control or thiol-blocked HSA. The reaction was biphasic. The first phase was approximately 20-fold faster than the second phase and first order in HSA-SOH and TNB (105 +/- 11 M-1 s-1, 25 degrees C, pH 7.4), allowing quantitative data on HSA-SOH formation and reactivity to be obtained. Exposure of reduced HSA (0.5 mM) to hydrogen peroxide (4 mM, 37 degrees C, 4 min) yielded 0.18 +/- 0.02 mol of HSA-SOH per mol of HSA. HSA-SH reacted with hydrogen peroxide at 2.7 +/- 0.7 M-1 s-1 (37 degrees C, pH 7.4), while HSA-SOH reacted at 0.4 +/- 0.2 M-1 s-1, yielding sulfinic acid (HSA-SO2H), as detected by mass spectrometry. The rate constants of HSA-SOH with targets of analytical interest such as dimedone and sodium arsenite were determined. HSA-SOH did not react appreciably with the plasma reductants ascorbate or urate, nor with free basic amino acids. In contrast, HSA-SOH reacted rapidly with the plasma thiols cysteine, glutathione, homocysteine, and cysteinylglycine at 21.6 +/- 0.2, 2.9 +/- 0.5, 9.3 +/- 0.9, and 55 +/- 3 M-1 s-1 (25 degrees C, pH 7.4), respectively, supporting a role for HSA-SOH in the formation of mixed disulfides.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arsenites,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclohexanones,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrobenzoates,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfenic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/dimedone,
http://linkedlifedata.com/resource/pubmed/chemical/sodium arsenite,
http://linkedlifedata.com/resource/pubmed/chemical/thionitrobenzoic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
47
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
358-67
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pubmed:meshHeading |
pubmed-meshheading:18078330-Arsenites,
pubmed-meshheading:18078330-Cyclohexanones,
pubmed-meshheading:18078330-Humans,
pubmed-meshheading:18078330-Hydrogen Peroxide,
pubmed-meshheading:18078330-Molecular Structure,
pubmed-meshheading:18078330-Nitrobenzoates,
pubmed-meshheading:18078330-Oxidation-Reduction,
pubmed-meshheading:18078330-Serum Albumin,
pubmed-meshheading:18078330-Sodium Compounds,
pubmed-meshheading:18078330-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:18078330-Sulfenic Acids,
pubmed-meshheading:18078330-Sulfhydryl Compounds
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pubmed:year |
2008
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pubmed:articleTitle |
Reactivity of sulfenic acid in human serum albumin.
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pubmed:affiliation |
Laboratorios Enzimología, Facultad de Ciencias, Universidad de la República, Uruguay.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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