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Purification of Human IgG by Negative Chromatography on Omega-Aminohexyl-Agarose

Purification of Human IgG by Negative Chromatography on Omega-Aminohexyl-Agarose

Maria Cristiane Martins de Souza, Igor Tadeu Lazzarotto Bresolin, Sonia Maria Alves Bueno

J Chromatogr B Analyt Technol Biomed Life Sci. 2010 Feb 15;878(5-6):557-66.

PMID: 20079697

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP58856738	ω-Aminohexyl-Agarose		58856-73-8	Price

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