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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/35215
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dc.contributor.authorNakaie, C. R.-
dc.contributor.authorLanzer, D. A.-
dc.contributor.authorMalavolta, L.-
dc.contributor.authorCilli, Eduardo Maffud-
dc.contributor.authorRodrigues, M. M.-
dc.date.accessioned2014-05-20T15:24:38Z-
dc.date.accessioned2016-10-25T17:58:55Z-
dc.date.available2014-05-20T15:24:38Z-
dc.date.available2016-10-25T17:58:55Z-
dc.date.issued2003-07-01-
dc.identifierhttp://dx.doi.org/10.1016/S0003-2697(03)00196-9-
dc.identifier.citationAnalytical Biochemistry. San Diego: Academic Press Inc. Elsevier B.V., v. 318, n. 1, p. 39-46, 2003.-
dc.identifier.issn0003-2697-
dc.identifier.urihttp://hdl.handle.net/11449/35215-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/35215-
dc.description.abstractThis report demonstrates that due to the presence of residual reactive sites in their matrices, classical diethylaminoethyl-attaching commercial anion-exchanger resins such as DEAE-MacroPrep and DEAE-Sephadex A50 supports can be used for peptide synthesis. Moreover, due to the high stability of the peptide-resin bond in the final cleavage treatments, desired peptidyl-resins free of side-chain protecting groups, which enables them to be further used as solid support for affinity chromatography, can be obtained. To demonstrate this potentiality, a fragment corresponding to the antigenic and immunodominant epitope of sporozoites of the Plasmodium falciparum malaria parasite was synthesized in these traditional resins and antibody molecules generated against the peptide sequence were successfully retained in these peptidyl supports. Due to the maintenance of their original anion-exchange capacities, the present findings open the unique possibility of applying, simultaneously, dual anion-exchange and affinity procedures for purification of a variety of macromolecules. (C) 2003 Elsevier B.V. (USA). All rights reserved.en
dc.format.extent39-46-
dc.language.isoeng-
dc.publisherElsevier B.V.-
dc.sourceWeb of Science-
dc.subjectpeptidept
dc.subjectresinpt
dc.subjectpolymerpt
dc.subjection-exchange chromatographypt
dc.subjectaffinity chromatographypt
dc.titleUse of commercial anion-exchange resins as solid support for peptide synthesis and affinity chromatographyen
dc.typeoutro-
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUniv Fed São Paulo, Dept Biophys, BR-04044020 São Paulo, Brazil-
dc.description.affiliationUniv Fed São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil-
dc.description.affiliationUniv Estadual Paulista, Dept Bioquim & Tecnol Quim, BR-14800900 Araraquara, SP, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista, Dept Bioquim & Tecnol Quim, BR-14800900 Araraquara, SP, Brazil-
dc.identifier.doi10.1016/S0003-2697(03)00196-9-
dc.identifier.wosWOS:000183495900006-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofAnalytical Biochemistry-
dc.identifier.orcid0000-0002-4767-0904pt
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