Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/199240
Type: Artigo de periódico
Title: Purification Of Human Igg By Negative Chromatography On Omega-aminohexyl-agarose.
Author: de Souza, Maria Cristiane Martins
Bresolin, Igor Tadeu Lazzarotto
Bueno, Sonia Maria Alves
Abstract: The omega-aminohexyl diamine immobilized as ligand on CNBr- and bisoxirane-activated agarose gel was evaluated for the purification of human immunoglobulin G (IgG) from serum and plasma by negative affinity chromatography. The effects of matrix activation, buffer system, and feedstream on recovery and purity of IgG were studied. A one-step purification process using Hepes buffer at pH 6.8 allowed a similar recovery (69-76%) of the loaded IgG in the nonretained fractions for both matrices, but the purity was higher for epoxy-activated gel (electrophoretically homogeneous protein with a 6.5-fold purification). The IgG and human serum albumin (HSA) adsorption equilibrium studies showed that the adsorption isotherms of IgG and HSA obeyed the Langmuir-Freundlich and Langmuir models, respectively. The binding capacity of HSA was high (210.4 mg mL(-1) of gel) and a positive cooperativity was observed for IgG binding. These results indicate that immobilizing omega-aminohexyl using bisoxirane as coupling agent is a useful strategy for rapid purification of IgG from human serum and plasma.
Subject: Adsorption
Chromatography, Affinity
Humans
Hydrogen-ion Concentration
Immunoglobulin G
Ligands
Protein Binding
Sepharose
Serum Albumin
Rights: fechado
Identifier DOI: 10.1016/j.jchromb.2009.12.034
Address: http://www.ncbi.nlm.nih.gov/pubmed/20079697
Date Issue: 2010
Appears in Collections:Unicamp - Artigos e Outros Documentos

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