Solubility of disulfide-bonded proteins in the cytoplasm of Escherichia coli and its "oxidizing" mutant.

@article{Xiong2005SolubilityOD,
  title={Solubility of disulfide-bonded proteins in the cytoplasm of Escherichia coli and its "oxidizing" mutant.},
  author={Sheng Lin Xiong and Yi-fei Wang and Xiang-Rong Ren and Bing Nan Li and Mei-ying Zhang and Yong Luo and Ling Zhang and Qiu-ling Xie and Kuan-yuan Su},
  journal={World journal of gastroenterology},
  year={2005},
  volume={11 7},
  pages={1077-82}
}
AIM To study the influence of redox environment of Escherichia coli (E. coli) cytoplasm on disulfide bond formation of recombinant proteins. METHODS Bovine fibroblast growth factor (BbFGF) was selected as a model of simple proteins with a single disulfide bond and free cysteines. Anti-HBsAg single-chain Fv (HBscFv), an artificial multidomain protein, was… CONTINUE READING