4.5 Article

Adsorption of human serum proteins onto TREN-agarose: Purification of human IgG by negative chromatography

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.jchromb.2008.11.008

Keywords

Human IgG; Purification; Negative chromatography; Human serum; TREN-agarose gel

Funding

  1. CNPq (Brazil)
  2. FAPESP (Brazil)

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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. (C) 2008 Elsevier B.V. All rights reserved.

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