Purification of Fusion Proteins by Affinity Chromatography on Glutathione Resin
Abstract
Fusion proteins that contain a glutathione S-transferase (GST) moiety can be purified to near homogeneity by affinity chromatography on glutathione-linked resins. Glutathione immobilized on a chromatography matrix, such as agarose or Sepharose, acts as a substrate for the GST moiety of fusion proteins. Contaminating proteins are washed away, and the bound GST fusion proteins are then readily displaced from the resin by elution with buffers containing free glutathione.
Footnotes
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From the Molecular Cloning collection, edited by Michael R. Green and Joseph Sambrook.
