Document Detail


Formation and reactions of sulfenic acid in human serum albumin.
MedLine Citation:
PMID:  20513474     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Protein sulfenic acids (R-SOH) are receiving increased interest as intermediates in redox processes. Human serum albumin, the most abundant protein in plasma, possesses a single free thiol. We describe herein the different methodologies that we have employed to study the formation of sulfenic acid in this protein and characterize some of its properties, including reactions that lead to the formation of mixed disulfides and the sulfinic acid derivative. The thiol of albumin is oxidized by hydrogen peroxide and peroxynitrite to a relatively stable sulfenic acid, which can be detected through different strategies including reduction with sodium arsenite and reaction with glutathione. Dimedone trapping followed by mass spectrometry analysis confirmed the modification. The challenge of obtaining quantitative data regarding albumin sulfenic acid has been approached using the yellow thiol thionitrobenzoate. A careful analysis has led to the determination of the rate constants of the reactions of sulfenic acid with analytical probes and with possible biological targets such as plasma thiols, which lead to mixed disulfides, and hydrogen peroxide, which overoxidizes the sulfenic to sulfinic acid. Our results support the concept that sulfenic acid is a central intermediate in the formation of oxidized albumin species that are present in circulating albumin and increase under pathological conditions.
Authors:
Beatriz Alvarez; Sebastián Carballal; Lucía Turell; Rafael Radi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Methods in enzymology     Volume:  473     ISSN:  1557-7988     ISO Abbreviation:  Meth. Enzymol.     Publication Date:  2010  
Date Detail:
Created Date:  2010-06-01     Completed Date:  2010-09-02     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0212271     Medline TA:  Methods Enzymol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  117-36     Citation Subset:  IM    
Copyright Information:
Copyright (c) 2010 Elsevier Inc. All rights reserved.
Affiliation:
Laboratorio de Enzimología, Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay.
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MeSH Terms
Descriptor/Qualifier:
Arsenites / chemistry,  pharmacology
Catalysis
Cyclohexanones / chemistry,  pharmacology
Glutathione / metabolism,  pharmacology
Humans
Mass Spectrometry
Models, Biological
Oxidation-Reduction
Serum Albumin / analysis,  chemistry,  metabolism*
Sodium Compounds / chemistry,  pharmacology
Sulfenic Acids / chemistry,  metabolism*
Sulfhydryl Compounds / analysis,  metabolism
Grant Support
ID/Acronym/Agency:
//Howard Hughes Medical Institute
Chemical
Reg. No./Substance:
0/Arsenites; 0/Cyclohexanones; 0/Serum Albumin; 0/Sodium Compounds; 0/Sulfenic Acids; 0/Sulfhydryl Compounds; 126-81-8/dimedone; 13768-07-5/sodium arsenite; 70-18-8/Glutathione

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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