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Publicação:
Metal ions bound to the human milk immunoglobulin A: Metalloproteomic approach

dc.contributor.authorCosta Pozzi, Carla Mariane [UNESP]
dc.contributor.authorBraga, Camila Pereira [UNESP]
dc.contributor.authorSouza Vieira, Jose Cavalcante [UNESP]
dc.contributor.authorCavecci, Bruna [UNESP]
dc.contributor.authorQueiroz, Joao Vitor de [UNESP]
dc.contributor.authorBarbosa, Herbert de Souza
dc.contributor.authorZezzi Arruda, Marco Aurelio
dc.contributor.authorGozzo, Fabio Cesar
dc.contributor.authorPadilha, Pedro de Magalhaes [UNESP]
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.date.accessioned2015-03-18T15:53:30Z
dc.date.available2015-03-18T15:53:30Z
dc.date.issued2015-01-01
dc.description.abstractThe presence of calcium, iron, and zinc bound to human milk secretory IgA (sIgA) was investigated. The sIgA components were first separated by two-dimensional polyacrylamide gel electrophoresis and then identified by electrospray ionization-tandem mass spectrometry (ESI MS MS). The metal ions were detected by flame atomic absorption spectrometry after acid mineralization of the spots. The results showed eight protein spots corresponding to the IgA heavy chain constant region. Another spot was identified as the transmembrane secretory component. Calcium was bound to both the transmembrane component and the heavy chain constant region, while zinc was bound to the heavy chain constant region and iron was not bound with the identified proteins. The association of a metal ion with a protein is important for a number of reasons, and therefore, the findings of the present study may lead to a better understanding of the mechanisms of action and of additional roles that sIgA and its components play in human milk. (C) 2014 Elsevier Ltd. All rights reserved.en
dc.description.affiliationSao Paulo State Univ, UNESP, Inst Biosci, BR-18618970 Botucatu, SP, Brazil
dc.description.affiliationUniv Estadual Campinas, UNICAMP, Inst Chem, Campinas, SP, Brazil
dc.description.affiliationUnespSao Paulo State Univ, UNESP, Inst Biosci, BR-18618970 Botucatu, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipIdFAPESP: 10/51332-5
dc.description.sponsorshipIdFAPESP: 11/03291-0
dc.format.extent492-497
dc.identifierhttp://dx.doi.org/10.1016/j.foodchem.2014.06.040
dc.identifier.citationFood Chemistry. Oxford: Elsevier Sci Ltd, v. 166, p. 492-497, 2015.
dc.identifier.doi10.1016/j.foodchem.2014.06.040
dc.identifier.issn0308-8146
dc.identifier.lattes6981448637456391
dc.identifier.urihttp://hdl.handle.net/11449/116552
dc.identifier.wosWOS:000342654200066
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofFood Chemistry
dc.relation.ispartofjcr4.946
dc.relation.ispartofsjr1,793
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectFlame atomic absorption spectrometryen
dc.subjectHuman milken
dc.subjectElectrospray ionization-tandem massen
dc.subjectspectrometryen
dc.subjectMetalloproteomicsen
dc.subjectSecretory IgAen
dc.subjectTwo-dimensional electrophoresisen
dc.titleMetal ions bound to the human milk immunoglobulin A: Metalloproteomic approachen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
dspace.entity.typePublication
unesp.author.lattes6981448637456391
unesp.author.orcid0000-0003-4179-0574[9]
unesp.author.orcid0000-0001-5447-8913[4]
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Biociências, Botucatupt
unesp.departmentQuímica e Bioquímica - IBBpt

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