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Isolation and Characterization Of Chimeric Human Fc-expressing Proteins Using Protein A Membrane Adsorbers And A Streamlined Workflow
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Adsorption of human serum proteins onto TREN-agarose: purification of human IgG by negative chromatography

Igor Tadeu Lazzarotto Bresolin1, Mariana Borsoi-Ribeiro, Juliana Rodrigues Caro

  • 1Department of Biotechnological Processes, School of Chemical Engineering, University of Campinas, UNICAMP, Campinas, SP, Brazil.

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
|November 28, 2008
PubMed

Tris(2-aminoethyl)amine (TREN) - a chelating agent used in IMAC - immobilized onto agarose gel was evaluated for the purification of IgG from human serum by negative chromatography. A one-step purification process allowed the recovery of 73.3% of the loaded IgG in the nonretained fractions with purity of 90-95% (based on total protein concentration and nephelometric analysis of albumin, transferrin, and immunoglobulins A, G, and M). The binding capacity was relatively high (66.63 mg of human serum protein/mL). These results suggest that this negative chromatography is a potential technique for purification of IgG from human serum.

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