Preparation, Analysis and Use of an Affinity Adsorbent for the Purification of GST Fusion Protein
Forde, Gareth M. (2008) Preparation, Analysis and Use of an Affinity Adsorbent for the Purification of GST Fusion Protein. In Zachariou, Michael (Ed.) Affinity Chromatography: Methods and Protocols [2nd ed.]. Humana Press (Springer), Totowa, NJ, pp. 125-136.
Methods are presented for the preparation, ligand density analysis and use of an affinity adsorbent for the purification of a glutathione S-transferase (GST) fusion protein in packed and expanded bed chromatographic processes. The protein is composed of GST fused to a zinc finger transcription factor (ZnF). Glutathione, the affinity ligand for GST purification, is covalently immobilized to a solid-phase adsorbent (Streamline™). The GST–ZnF fusion protein displays a dissociation constant of 0.6 x10-6 M to glutathione immobilized to Streamline™. Ligand density optimization, fusion protein elution conditions (pH and glutathione concentration) and ligand orientation are briefly discussed.
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|Item Type:||Book Chapter|
|Keywords:||GST fusion protein, affinity purification, chromatography, expanded bed adsorption|
|Divisions:||Current > Schools > School of Chemistry, Physics & Mechanical Engineering
Current > QUT Faculties and Divisions > Science & Engineering Faculty
|Deposited On:||09 Feb 2015 23:21|
|Last Modified:||13 Feb 2015 04:31|
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