Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/200801
Type: Artigo de periódico
Title: Behavior Of Human Immunoglobulin G Adsorption Onto Immobilized Cu(ii) Affinity Hollow-fiber Membranes.
Author: Borsoi-Ribeiro, Mariana
Bresolin, Igor Tadeu Lazzarotto
Vijayalakshmi, Mookambeswaran
Bueno, Sônia Maria Alves
Abstract: Iminodiacetic 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 298.4 mg g(-1) dry weight for PEVA-TREN-Cu(II) and PEVA-IDA-Cu(II), respectively) was somewhat higher than the equilibrium capacity (9.2 and 73.3 mg g(-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.
Subject: Adsorption
Cations, Divalent
Chelating Agents
Chromatography, Affinity
Copper
Epichlorohydrin
Epoxy Compounds
Ethylenediamines
Imino Acids
Immunoglobulin G
Kinetics
Membranes, Artificial
Polyvinyls
Protein Binding
Solutions
Thermodynamics
Cu(ii)
Imac
Adsorption
Affinity Membranes
Human Igg
Tris(2-aminoethyl)amine
Citation: Journal Of Molecular Recognition : Jmr. v. 26, n. 10, p. 514-20, 2013-Oct.
Rights: fechado
Identifier DOI: 10.1002/jmr.2296
Address: http://www.ncbi.nlm.nih.gov/pubmed/23996494
Date Issue: 2013
Appears in Collections:Unicamp - Artigos e Outros Documentos

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