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Fig. 1 | Microbial Cell Factories

Fig. 1

From: Direct expression of active human tissue inhibitors of metalloproteinases by periplasmic secretion in Escherichia coli

Fig. 1

Direct production of soluble (N-)TIMPs in E. coli periplasm and their biochemical and cellular function characterizations. Unfolded TIMPs with free cysteines were expressed in cytoplasm and secreted to periplasmic space, where periplasmic chaperones, especially DsbC (a disulfide isomerase), resolved incorrect disulfide bonds, resulting in properly folded TIMPs. Following enzymatic and osmotic treatments, high yields of soluble (N-)TIMPs were purified from periplasmic preparation. The purified (N-)TIMPs were subjected to function tests both biochemically and in the cellular context. GPC gel permeation chromatography

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Microbial Cell Factories

ISSN: 1475-2859

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