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Jacalin interaction with human immunoglobulin A1 and bovine immunoglobulin G1: Affinity constant determined by piezoelectric biosensoring

dc.contributor.authorPedroso, Mariele M.
dc.contributor.authorPesquero, Naira C. [UNESP]
dc.contributor.authorThomaz, Sandra M. O. [UNESP]
dc.contributor.authorRoque-Barreira, Maria C.
dc.contributor.authorFaria, Ronaldo C.
dc.contributor.authorBueno, Paulo Roberto [UNESP]
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2014-05-20T15:31:25Z
dc.date.available2014-05-20T15:31:25Z
dc.date.issued2012-03-01
dc.description.abstractThe affinity of the d-galactose-binding lectin from Artocarpus heterophyllus lectin, known as jacalin, with immonuglobulins (Igs) was determined by biofunctionalization of a piezoelectric transducer. This piezoelectric biofunctionalized transducer was used as a mass-sensitive analytical tool, allowing the real-time binding analysis of jacalin-human immunoglobulin A1 (IgA(1)) and jacalin-bovine IgG(1) interactions from which the apparent affinity constant was calculated. The strategy was centered in immobilizing jacalin on the gold electrode's surface of the piezoelectric crystal resonator using appropriate procedures based on self-assembling of 11-mercaptoundecanoic acid and 2-mercaptoethanol thiol's mixture, a particular immobilization strategy by which it was possible to avoid cross-interaction between the proteins over electrode's surface. The apparent affinity constants obtained between jacalin-human IgA(1) and jacalin-bovine IgG(1) differed by 1 order of magnitude [(8.0 +/- 0.9) x 10(5) vs (8.3 +/- 0.1) x 10(6) L mol(-1)]. on the other hand, the difference found between human IgA(1) and human IgA(2) interaction with jacalin, eight times higher for IgA(1), was attributed to the presence of O-linked glycans in the IgA(1) hinge region, which is absent in IgA(2). Specific interaction of jacalin with O-glycans, proved to be present in the human IgA(1) and hypothetically present in bovine IgG(1) structures, is discussed as responsible for the obtained affinity values.en
dc.description.affiliationUniversidade Federal de São Carlos (UFSCar), Dept Quim, BR-13560905 São Paulo, Brazil
dc.description.affiliationUniv Estadual Paulista, Inst Quim, Dept Quim Fis, BR-14800900 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Fac Med Ribeirao Preto, Dept Biol Celular & Mol & Bioagentes Patogen, BR-14049900 São Paulo, Brazil
dc.description.affiliationUnespUniv Estadual Paulista, Inst Quim, Dept Quim Fis, BR-14800900 São Paulo, 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: 10/05331-7
dc.format.extent326-331
dc.identifierhttp://dx.doi.org/10.1093/glycob/cwr099
dc.identifier.citationGlycobiology. Cary: Oxford Univ Press Inc, v. 22, n. 3, p. 326-331, 2012.
dc.identifier.doi10.1093/glycob/cwr099
dc.identifier.issn0959-6658
dc.identifier.lattes0477045906733254
dc.identifier.orcid0000-0003-2827-0208
dc.identifier.urihttp://hdl.handle.net/11449/40558
dc.identifier.wosWOS:000299747400002
dc.language.isoeng
dc.publisherOxford University Press
dc.relation.ispartofGlycobiology
dc.relation.ispartofjcr3.664
dc.relation.ispartofsjr1,493
dc.rights.accessRightsAcesso restritopt
dc.sourceWeb of Science
dc.subjectApparent affinity constanten
dc.subjectimmunoglobulinen
dc.subjectjacalinen
dc.subjectlectinen
dc.subjectQCMen
dc.titleJacalin interaction with human immunoglobulin A1 and bovine immunoglobulin G1: Affinity constant determined by piezoelectric biosensoringen
dc.typeArtigopt
dcterms.licensehttp://www.oxfordjournals.org/access_purchase/self-archiving_policyb.html
dcterms.rightsHolderOxford Univ Press Inc
dspace.entity.typePublication
relation.isOrgUnitOfPublicationbc74a1ce-4c4c-4dad-8378-83962d76c4fd
relation.isOrgUnitOfPublication.latestForDiscoverybc74a1ce-4c4c-4dad-8378-83962d76c4fd
unesp.author.lattes0477045906733254[6]
unesp.author.orcid0000-0003-2827-0208[6]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Química, Araraquarapt
unesp.departmentFísico-Química - IQARpt

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