Purification of Fusion Proteins by Affinity Chromatography on Glutathione Resin

Clara L. Kielkopf; William Bauer; Ina L. Urbatsch

doi:10.1101/pdb.prot102202

Purification of Fusion Proteins by Affinity Chromatography on Glutathione Resin

Clara L. Kielkopf
, William Bauer
, Ina L. Urbatsch

Pediatrics

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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.

Original language	English
Pages (from-to)	217-224
Number of pages	8
Journal	Cold Spring Harbor Protocols
Volume	2020
Issue number	6
DOIs	https://doi.org/10.1101/pdb.prot102202
State	Published - Jun 2020

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title = "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.",

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N2 - 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.

AB - 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.

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DO - 10.1101/pdb.prot102202

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JO - Cold Spring Harbor Protocols

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Purification of Fusion Proteins by Affinity Chromatography on Glutathione Resin

Abstract

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