Artículos de revistas
Adsorption Of Human Serum Proteins Onto Tren-agarose: Purification Of Human Igg By Negative Chromatography.
Registro en:
Journal Of Chromatography. B, Analytical Technologies In The Biomedical And Life Sciences. v. 877, n. 1-2, p. 17-23, 2009-Jan.
1570-0232
10.1016/j.jchromb.2008.11.008
19036647
Autor
Bresolin, Igor Tadeu Lazzarotto
Borsoi-Ribeiro, Mariana
Caro, Juliana Rodrigues
dos Santos, Francine Petit
de Castro, Marina Polesi
Bueno, Sonia Maria Alves
Institución
Resumen
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. 877 17-23