Reduction of bovine immunoglobulin contamination from monoclonal antibodies by SOURCE 15PHE chromatography.
The presence of bovine immunoglobulin in cell culture media, and its nature as a polyclonal antibody, imposes increasing difficulties in resolution from the MAb intended for in vivo human applications. Particular difficulties are encountered when murine MAbs are the target antibody. This study presents model cases to simulate this problem, and suggests an efficient method for reduction of bovine IgG (BGG) from MAb preparations. Utilizing the new small particle size hydrophobic interaction chromatography resin, SOURCE 15PHE, up to complete resolution was achieved with a chimeric MAb. A 17-fold reduction of BGG was achieved with a murine MAb. In both cases, high recoveries of the MAb were obtained. The general applicability of the method is suggested.
Grunfeld
H
H
Pharmacia Biotech, Inc., Piscataway, NJ 08855, USA.
Moore
P
P
D000818:Animals; D000911:Antibodies, Monoclonal / Q000302:isolation & purification*; D001426:Bacterial Proteins; D002417:Cattle; D002846:Chromatography, Affinity; D002853:Chromatography, Liquid / Q000379:methods*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000302:isolation & purification*; D051379:Mice; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D005719:gamma-Globulins / Q000302:isolation & purification
D000911:Antibodies, Monoclonal; D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D007074:Immunoglobulin G; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A; D005719:gamma-Globulins