Behavior of human immunoglobulin G adsorption onto immobilized Cu(II) affinity hollow-fiber membranes
Nenhuma Miniatura disponível
Data
2013-10-01
Autores
Borsoi-Ribeiro, Mariana
Lazzarotto Bresolin, Igor Tadeu [UNIFESP]
Vijayalakshmi, Mookambeswaran
Alves Bueno, Sonia Maria
Orientadores
Tipo
Artigo
Título da Revista
ISSN da Revista
Título de Volume
Resumo
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 298.4mgg(-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.
Descrição
Citação
Journal of Molecular Recognition. Hoboken: Wiley-Blackwell, v. 26, n. 10, p. 514-520, 2013.