Further characterization of the subunits of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) by SDS-PAGE electrophoresis and MALDI-TOF-MS

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dc.contributor.authorCarvalho, Francisco Adriano O.
dc.contributor.authorCarvalho, José Wilson P.
dc.contributor.authorSantiago, Patrícia S. [UNESP]
dc.contributor.authorTabak, Marcel
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:26:06Z
dc.date.available2014-05-27T11:26:06Z
dc.date.issued2011-11-01
dc.description.abstractFurther characterization of hemoglobin of Glossoscolex paulistus (HbGp) subunits was performed based on SDS-PAGE, size exclusion chromatography (SEC) and MALDI-TOF-MS analysis. SDS-PAGE has shown a total of four linker chains, two quite intense and two of lower intensity. HbGp fractions (I-VI), obtained by size exclusion chromatography (SEC), from oligomeric dissociation at alkaline pH 9.6, were monitored. Fraction I is identical to the whole protein. The monomeric chains c, obtained from the trimer abc reduction, present four isoforms with MM 17,336 Da, 17,414 Da, 17,546 Da and 17,620 Da. Furthermore, the trimer subunit presents two isoforms, T 1 and T 2, with MM 51,200 ± 60 and 51,985 ± 50 Da, respectively. Based on SDS-PAGE, the linker chains seem to be distributed along the different fractions of the SEC chromatogram, appearing along the peaks corresponding to fractions I-V. The fraction IV contains, predominantly, trimers with some linkers contamination. The strong interaction of linker chains L with the trimers abc, makes it difficult to obtain these subunits in pure form. The monomer d in fraction VI appears to be quite pure, in agreement with previous studies. © 2011 Elsevier Ltd. All rights reserved.en
dc.description.affiliationInstituto de Química de São Carlos Universidade de São Paulo, São Carlos, SP
dc.description.affiliationUniversidade Estadual Paulista Júlio de Mesquita Filho Campus Experimental de Registro, SP
dc.description.affiliationUnespUniversidade Estadual Paulista Júlio de Mesquita Filho Campus Experimental de Registro, SP
dc.format.extent2144-2151
dc.identifierhttp://dx.doi.org/10.1016/j.procbio.2011.08.013
dc.identifier.citationProcess Biochemistry, v. 46, n. 11, p. 2144-2151, 2011.
dc.identifier.doi10.1016/j.procbio.2011.08.013
dc.identifier.file2-s2.0-80053956145.pdf
dc.identifier.issn1359-5113
dc.identifier.lattes6705367010662087
dc.identifier.orcid0000-0002-6205-9441
dc.identifier.scopus2-s2.0-80053956145
dc.identifier.urihttp://hdl.handle.net/11449/72767
dc.language.isoeng
dc.relation.ispartofProcess Biochemistry
dc.relation.ispartofjcr2.616
dc.relation.ispartofsjr0,761
dc.rights.accessRightsAcesso aberto
dc.sourceScopus
dc.subjectElectrophoresisen
dc.subjectExtracellular hemoglobinen
dc.subjectGlossosocolex paulistusen
dc.subjectMALDI-TOF-MSen
dc.subjectSubunits characterizationen
dc.subjectSubunits molecular massesen
dc.subjectExtracellularen
dc.subjectMALDI TOF MSen
dc.subjectAlkalinityen
dc.subjectCharacterizationen
dc.subjectChromatographic analysisen
dc.subjectGel permeation chromatographyen
dc.subjectHemoglobinen
dc.subjectInductively coupled plasmaen
dc.subjectOligomersen
dc.subjectSize exclusion chromatographyen
dc.subjectGlossoscolexen
dc.titleFurther characterization of the subunits of the giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) by SDS-PAGE electrophoresis and MALDI-TOF-MSen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
unesp.author.lattes6705367010662087[3]
unesp.author.orcid0000-0002-6205-9441[3]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Agrárias do Vale do Ribeira, Registropt
unesp.departmentEngenharia Agronômica - FCAVRpt

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