1994
DOI: 10.1038/nbt1194-1113
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Large Scale, In Situ Isolation of Periplasmic IGF–I from E. coli

Abstract: Human insulin-like growth factor I (IGF-I) accumulates in both folded and aggregated forms in the fermentation medium and cellular periplasmic space when expressed in E. coli with an endogenous secretory signal sequence. Due to its heterogeneity in form and location, low yield of IGF-I was obtained using a typical refractile body recovery strategy. To enhance recovery yield, a new procedure was developed to solubilize and extract IGF-I from cells while in fermentation broth. This method, called in situ solubil… Show more

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Cited by 95 publications
(55 citation statements)
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“…3). This agrees well with shake flask experiments and osmotic shock treatment of the cells (23). A similar proportion of denaturant-extractable polypeptide was measured in dsbC null strains (15%, Fig.…”
Section: Resultssupporting
confidence: 76%
See 1 more Smart Citation
“…3). This agrees well with shake flask experiments and osmotic shock treatment of the cells (23). A similar proportion of denaturant-extractable polypeptide was measured in dsbC null strains (15%, Fig.…”
Section: Resultssupporting
confidence: 76%
“…Using this approach, a large increase in the total yield of the recombinant protein, human insulin-like growth factor-1 (IGF-I*), was observed after increasing the concentration of periplasmic thiol:disulfide oxidoreductase, DsbA, or DsbC. Although nearly all of the IGF-I accumulates in aggregates, there exists efficient methodology for the isolation and folding of these deposits (22,23).…”
mentioning
confidence: 99%
“…The chaotropic properties of urea make it useful as a strong denaturant. It has seen broad application for the solubilization and refolding of protein inclusion bodies obtained from Escherichia coli (e.g., [1][2][3][4][5][6]). There have been a smaller number of reports of urea used in conjunction with ion-exchange adsorption.…”
Section: Introductionmentioning
confidence: 99%
“…PEG interacts with the hydrophobic side chains exposed upon unfolding at high temperatures [46]. PEG has been successfully used for refolding of interferon [47], xylanase [48], and insulin-like growth factor (IGF-1) [49] from inclusion bodies.…”
Section: Polyethylene Glycol (Peg)mentioning
confidence: 99%