Adsorption of human serum proteins onto TREN-agarose: purification of human IgG by negative chromatography.
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.
Bresolin
Igor Tadeu Lazzarotto
IT
Department of Biotechnological Processes, School of Chemical Engineering, University of Campinas, UNICAMP, Campinas, SP, Brazil.
Borsoi-Ribeiro
Mariana
M
Caro
Juliana Rodrigues
JR
dos Santos
Francine Petit
FP
de Castro
Marina Polesi
MP
Bueno
Sonia Maria Alves
SM
D000327:Adsorption; D001798:Blood Proteins / Q000737:chemistry*; D002021:Buffers; D002853:Chromatography, Liquid / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007074:Immunoglobulin G / Q000302:isolation & purification*; D012680:Sensitivity and Specificity; D012685:Sepharose / Q000737:chemistry*
D001798:Blood Proteins; D002021:Buffers; D007074:Immunoglobulin G; D012685:Sepharose