Rapid purification of a recombinant protein using tandem radial flow ion-exchange column chromatography. |
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Authors: | J E McCartney |
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Institution: | Creative BioMolecules, Inc., Hopkinton, MA 01748. |
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Abstract: | 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. |
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