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dc.contributor.authorBorsoi-Ribeiro, Mariana
dc.contributor.authorLazzarotto Bresolin, Igor Tadeu [UNIFESP]
dc.contributor.authorVijayalakshmi, Mookambeswaran
dc.contributor.authorAlves Bueno, Sonia Maria
dc.identifier.citationJournal of Molecular Recognition. Hoboken: Wiley-Blackwell, v. 26, n. 10, p. 514-520, 2013.
dc.description.abstractIminodiacetic acid (IDA) and tris(2-aminoethyl)amine (TREN) chelating ligands were immobilized on poly(ethylene vinyl alcohol) (PEVA) hollow-fiber membranes after activation with epichlorohydrin or butanediol diglycidyl ether (bisoxirane). the affinity membranes complexed with Cu(II) were evaluated for adsorption of human immunoglobulin G (IgG). the effects of matrix activation and buffer system on adsorption of IgG were studied. Isotherms of batch IgG adsorption onto finely cut membranes showed that neither of the chelates, IDA-Cu(II) or TREN-Cu(II), had a Langmuirean behavior with negative cooperativity for IgG binding. A comparison of equilibrium and dynamic maximum capacities showed that the dynamic capacity for a mini-cartridge in a cross-flow filtration mode (52.5 and 298.4mgg(-1) dry weight for PEVA-TREN-Cu(II) and PEVA-IDA-Cu(II), respectively) was somewhat higher than the equilibrium capacity (9.2 and 73.3mgg(-1) dry weight for PEVA-TREN-Cu(II) and PEVA-IDA-Cu(II), respectively). When mini-cartridges were used, the dynamic adsorption capacity of IDA-Cu(II) was the same for both mini-cartridge and agarose gel. Copyright (c) 2013 John Wiley & Sons, Ltd.en
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.relation.ispartofJournal of Molecular Recognition
dc.rightsAcesso restrito
dc.subjecthuman IgGen
dc.subjectaffinity membranesen
dc.titleBehavior of human immunoglobulin G adsorption onto immobilized Cu(II) affinity hollow-fiber membranesen
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Technol Compiegne
dc.contributor.institutionVIT Univ Vellore
dc.description.affiliationUniv Estadual Campinas, UNICAMP, Sch Chem Engn, BR-13083970 Campinas, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, UNIFESP, Dept Exact & Earth Sci, BR-09913030 São Paulo, Brazil
dc.description.affiliationUniv Technol Compiegne, Lab Interact Mol & Technol Separat, F-60205 Compiegne, France
dc.description.affiliationVIT Univ Vellore, Ctr Bioseparat Technol, Vellore 632014, Tamil Nadu, India
dc.description.affiliationUnifespUniversidade Federal de São Paulo, UNIFESP, Dept Exact & Earth Sci, BR-09913030 São Paulo, Brazil
dc.description.sourceWeb of Science

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