Navegando por Palavras-chave "IMAC"

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    Behavior of human immunoglobulin G adsorption onto immobilized Cu(II) affinity hollow-fiber membranes
    (Wiley-Blackwell, 2013-10-01) Borsoi-Ribeiro, Mariana; Lazzarotto Bresolin, Igor Tadeu [UNIFESP]; Vijayalakshmi, Mookambeswaran; Alves Bueno, Sonia Maria; Universidade Estadual de Campinas (UNICAMP); Universidade Federal de São Paulo (UNIFESP); Univ Technol Compiegne; VIT Univ Vellore
    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.
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    The effect of NaCl on the adsorption of human IgG onto CM-Asp-PEVA hollow fiber membrane-immobilized nickel and cobalt metal ions
    (Springer, 2014-08-01) Pavan, Gisele Luiza; Lazzarotto Bresolin, Igor Tadeu [UNIFESP]; Borsoi-Ribeiro, Mariana; Vijayalakshmi, Mookambesvaran; Alves Bueno, Sonia Maria; Universidade Estadual de Campinas (UNICAMP); Universidade Federal de São Paulo (UNIFESP); VIT Univ
    Over the past decade, immobilized metal-affinity adsorbents have attracted increasing interest for purification of natural and recombinant immunoglobulin G (IgG). in this work, nickel and cobalt metal ions complexed with CM-Asp (carboxymethylaspartate) immobilized on poly(ethylenevinyl alcohol) (PEVA) hollow fiber membranes were evaluated for purification of human IgG from serum. the buffer system and NaCl had important effects on human serum protein adsorption in both adsorbents. Efficient purification of IgG was accomplished in sodium phosphate buffer without NaCl at pH 7.0. Under this condition, the electrostatic interactions are important for adsorption. the Ni(II)-CM-Asp-PEVA had a protein adsorption capacity of 17.5 mg of IgG mL(-1) fiber when human serum diluted was loaded in crossflow filtration mode and the eluted IgG had a purity of 82.6 % (based on total protein and IgG, IgM, HSA, and Trf nephelometric analysis). Fitting the experimental IgG adsorption data to the Langmuir and Langmuir-Freundlich models showed that Ni(II)-CM-Asp and Co(II)-CM-Asp had Langmuirean and non-Langmuirean behavior, respectively, with positive cooperativity for IgG-Co(II)-CM-Asp binding, probably due to multipoint interactions (n = 2.12 +/- A 0.31). Thus, these membranes can be considered as alternative adsorbents for the purification or depletion of IgG from human serum.