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Article

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

World journal of gastroenterology - 21 Feb 2005

Xiong Sheng, Wang Yi-Fei, Ren Xiang-Rong, Li Bing, Zhang Mei-Ying, Luo Yong, Zhang Ling, Xie Qiu-Ling, Su Kuan-Yuan

Abstract excerpt

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 selected as the model molecule of complex protein with 2...

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Identifiers

PMID: 15742420
DOI: 10.3748/wjg.v11.i7.1077
PMCID: PMC4250777

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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