Rapid purification of a recombinant protein using tandem radial flow ion-exchange column chromatography.
Tandem radial flow anion- and cation-exchange columns were used to partially purify and concentrate a dilute recombinant protein that had been refolded in vitro after production as insoluble inclusion bodies in E. coli. The refolded sample was first passed through a Q-Sepharose Fast Flow column in order to remove the majority of E. coli contaminating proteins and endotoxins, then purified on an S-Sepharose Fast Flow column connected to the outlet of the Q-Sepharose column. This tandem arrangement enabled the rapid processing of multiple preparations of refolded material during production method development.
McCartney
J E
JE
Creative BioMolecules, Inc., Hopkinton, MA 01748.
D002852:Chromatography, Ion Exchange / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D011994:Recombinant Proteins / Q000302:isolation & purification*
D011994:Recombinant Proteins