Abstract
DsbA and DsbC, members of the thioredoxin super-family of redox proteins, which are expressed in the periplasmic space of Escherichia coli, were cloned into and successfully secreted from Brevibacillus choshinensis at ∼100 μg ml−1. Both proteins were active in exchanging disulfide bonds of bovine insulin in vitro. Furthermore, DsbA secreted by B. choshinensis promoted the conversion of non-native human epidermal growth factor to the native form.
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Tanaka, R., Hashimoto, M., Ishibashi, M. et al. Secretion of Escherichia coli DsbA and DsbC proteins from Brevibacillus choshinensis: stimulation of human epidermal growth factor production. Biotechnology Letters 23, 1853–1857 (2001). https://doi.org/10.1023/A:1012798406359
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DOI: https://doi.org/10.1023/A:1012798406359