Citation: Dong Xin Zhao, Zhong Xian Huang. Effect of arginine on stability of GST-ZNF191(243-368)[J]. Chinese Chemical Letters, ;2007, 18(3): 355-356. doi: 10.1016/j.cclet.2007.01.017 shu

Effect of arginine on stability of GST-ZNF191(243-368)

Chemical Biology Lab, Department of Chemistry, Fudan University, Shanghai 200433, China

Received Date: 30 August 2006

For better understanding the chemical or biological information of ZNF191 (243-368), we expressed the fusion protein of GST and ZNF191(243-368), and used it to obtain the binding DNA sequence of this zinc finger protein. But in the process of expression and purification, we found this fusion protein slowly degradated. For resolving this problem, we simultaneously added charged amino acids L-Arg and L-Glu to the solution of fusion protein, and demonstrated that this method can dramatically increase the stability of this fusion protein. This method can make the fusion protein suitable for the continuous works, especially for situations where high protein concentration and long-term stability without precipitate and degradation of protein are required.
- ZNF191(243-368),
- GST,
- Stability,
- L-Arg,
- L-Glu
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