Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1216444 | Journal of Chromatography B | 2009 | 7 Pages |
Abstract
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Igor Tadeu Lazzarotto Bresolin, Mariana Borsoi-Ribeiro, Juliana Rodrigues Caro, Francine Petit dos Santos, Marina Polesi de Castro, Sonia Maria Alves Bueno,