Taurine bromamine: A potent oxidant of tryptophan residues in albumin

dc.contributor.authorXimenes, Valdecir Farias [UNESP]
dc.contributor.authorda Fonseca, Luiz Marcos [UNESP]
dc.contributor.authorde Almeida, Ana Carolina [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:23:57Z
dc.date.available2014-05-20T13:23:57Z
dc.date.issued2011-03-15
dc.description.abstractTaurine is the most abundant free amino acid in leukocytes and can react with HOBr to produce taurine bromamine (Tau-NHBr). The aim of this study was to assess the ability of Tau-NHBr to oxidize tryptophan, either free or as a residue in albumin. We have demonstrated that Tau-NHBr is a powerful oxidant for tryptophan. Importantly, in comparison to taurine chloramine, HOCl or HOBr, Tau-NHBr exhibits a degree of selectivity for tryptophan. Oxidation of albumin by Tau-NHBr resulted in emission of light, and the quantum yield was more than 10-fold more efficient than that of the other oxidants. The fluorescence band corresponding to oxidized albumin (lambda(ex) 350/lambda(em) 450), which is characteristic of the formation of formylkynurenine, was significantly higher in reactions using Tau-NHBr. Excitation of the fluorescent probe 8-anilino-1-naphthalenesulfonate at 295 nm was used to assess the depletion of tryptophan residues in albumin. Results from this experiment further supported a higher efficiency of oxidation of tryptophan residues by Tau-NHBr. Other parameters of protein oxidation, including cysteine depletion and formation of carbonyl groups, were not significantly different between the oxidants tested. In conclusion, these results indicate that Tau-NHBr has a higher affinity for tryptophan residues in proteins. (C) 2010 Elsevier B.V. All rights reserved.en
dc.description.affiliationUNESP Univ Estadual Paulista, Dept Quim, Fac Ciencias, BR-17033360 São Paulo, SP, Brazil
dc.description.affiliationUNESP Univ Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.description.affiliationUnespUNESP Univ Estadual Paulista, Dept Quim, Fac Ciencias, BR-17033360 São Paulo, SP, Brazil
dc.description.affiliationUnespUNESP Univ Estadual Paulista, Fac Ciencias Farmaceut, Dept Anal Clin, Araraquara, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent315-322
dc.identifierhttp://dx.doi.org/10.1016/j.abb.2010.12.026
dc.identifier.citationArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 507, n. 2, p. 315-322, 2011.
dc.identifier.doi10.1016/j.abb.2010.12.026
dc.identifier.issn0003-9861
dc.identifier.lattes4419635633356792
dc.identifier.urihttp://hdl.handle.net/11449/7323
dc.identifier.wosWOS:000288058000015
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.relation.ispartofjcr3.118
dc.relation.ispartofsjr1,350
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectTryptophanen
dc.subjectTaurine chloramineen
dc.subjectTaurine bromamineen
dc.subjectHypochlorous aciden
dc.subjectHypobromous aciden
dc.subjectAlbuminen
dc.titleTaurine bromamine: A potent oxidant of tryptophan residues in albuminen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes4419635633356792
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Farmacêuticas, Araraquarapt
unesp.departmentAnálises Clínicas - FCFpt

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