On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies

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dc.contributor.authorCarvalho, Jose Wilson P.
dc.contributor.authorSantiago, Patricia S. [UNESP]
dc.contributor.authorBatista, Tatiana
dc.contributor.authorGarrido Salmon, Carlos Ernesto
dc.contributor.authorBarbosa, Leandro R. S.
dc.contributor.authorItri, Rosangela
dc.contributor.authorTabak, Marcel
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T13:12:07Z
dc.date.available2014-05-20T13:12:07Z
dc.date.issued2012-04-01
dc.description.abstractGlossoscolex paulistus hemoglobin (HbGp) was studied by dynamic light scattering (DLS) and small angle X-ray scattering (SAXS). DLS melting curves were measured for met-HbGp at different concentrations. SAXS temperature studies were performed for oxy-, cyanomet- and met-HbGp forms, at several pH values. At pH 5.0 and 6.0, the scattering curves are identical from 20 to 60 degrees C, and R-g is 108 angstrom, independent of the oxidation form. At pH 7.0, protein denaturation and aggregation occurs above 55 degrees C and 60 degrees C, for oxy and met-HbGp, respectively. Cyanomet-HbGp, at pH 7.0, is stable up to 60 degrees C. At alkaline pH (8.0-9.0) and higher temperature, an irreversible dissociation process is observed, with a decrease of R-g, D-max and I(0). Analysis by p(r), obtained from GNOM, and OLIGOMER, was used to fit the SAXS experimental scattering curves by a combination of theoretical curves obtained for HbLt fragments from the crystal structure. Our results show clearly the increasing contribution of smaller molecular weight fragments, as a function of increasing pH and temperature, as well as, the order of thermal stabilities: cyanomet-> oxy- > met-HbGp. (C) 2012 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv São Paulo, Inst Quim São Carlos, São Carlos, SP, Brazil
dc.description.affiliationUniv Estadual Paulista, Registro, SP, Brazil
dc.description.affiliationUniv São Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Fis, Ribeirao Preto, SP, Brazil
dc.description.affiliationUniv São Paulo, Inst Fis, BR-01498 São Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Registro, 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.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 10/09719-0
dc.format.extent44-55
dc.identifierhttp://dx.doi.org/10.1016/j.bpc.2012.02.004
dc.identifier.citationBiophysical Chemistry. Amsterdam: Elsevier B.V., v. 163, p. 44-55, 2012.
dc.identifier.doi10.1016/j.bpc.2012.02.004
dc.identifier.issn0301-4622
dc.identifier.lattes6705367010662087
dc.identifier.orcid0000-0002-6205-9441
dc.identifier.urihttp://hdl.handle.net/11449/108
dc.identifier.wosWOS:000303225900005
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiophysical Chemistry
dc.relation.ispartofjcr1.870
dc.relation.ispartofsjr0,743
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectExtracellular hemoglobinen
dc.subjectGlossoscolex paulistusen
dc.subjectOligomeric dissociationen
dc.subjectThermal stabilityen
dc.subjectDLSen
dc.subjectSAXSen
dc.titleOn the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studiesen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.lattes6705367010662087[2]
unesp.author.orcid0000-0002-6205-9441[2]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Agrárias do Vale do Ribeira, Registropt

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