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Updated: Jun 17, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Published on: December 12, 2017
Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS
Hu Tao1, Wenjun Liu, Brandi N Simmons
1Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
Abstract:
We describe a rapid, simple, and efficient method for recovering glutathione S-transferase (GST)- and His6-tagged maltose binding protein (MBP) fusion proteins from inclusion bodies. Incubation of inclusion bodies with 10% sarkosyl effectively solubilized >95% of proteins, while high-yield recovery of sarkosyl-solubilized fusion proteins was obtained with a specific ratio of Triton X-100 and CHAPS. We demonstrate for the first time that this combination of three detergents significantly improves binding efficiency of GST and GST fusion proteins to gluthathione (GSH) Sepharose.
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