NDLI: Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation

Content Provider	PubMed Central
Author	Joly, John C. Leung, W. S. Swartz, James R.
Copyright Year	1998
Abstract	Transient overexpression of either DsbA or DsbC can double the yield of periplasmic insulin-like growth factor (IGF)-I in Escherichia coli to 8.5 g/liter. Strikingly, most of the overexpressed DsbA or DsbC is found in the reduced form, implying that enhanced disulfide isomerization is responsible for the substantial increase in IGF-I yield. All of the accumulated IGF-I has had the signal sequence removed, underscoring the secretion capacity of this organism as well as its utility for efficient production of polypeptide with the correct amino terminus. The overexpressed IGF-I constitutes approximately 30% of the total cell protein. Overproduction of active site mutants of DsbA instead of the wild-type gene do not produce this increase in yield. With wild-type levels of DsbA and DsbC, most of the secreted IGF-I is found in disulfide-linked aggregates, although 10% is soluble and about 5% is correctly folded. Contrary to expectations, overexpression of the disulfide oxidoreductases decreased the soluble fraction. Because the aggregated protein can be efficiently solubilized and refolded, the increased yield is a significant benefit for the production of IGF-I.
Starting Page	2773
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-03-17
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation.

Isolation of the human insulin-like growth factor genes: insulin-like growth factor II and insulin genes are contiguous.

Separation and characterization of modified variants of recombinant human insulin-like growth factor I derived from a fusion protein secreted from Escherichia coli.

Effects of recombinant insulin-like growth factor I on insulin secretion and renal function in normal human subjects.

Effects of recombinant insulin-like growth factor I on insulin secretion and renal function in normal human subjects.

Recombinant human insulin-like growth factor I induces its own specific carrier protein in hypophysectomized and diabetic rats.

Expression of Recombinant Human Insulin-like Growth Factor Type 1 (rhIGF-1) in Escherichia coli

Expression and efficient purification of tag-cleaved active recombinant human insulin-like growth factor-II from Escherichia coli

Recombinant human insulin-like growth factor I stimulates growth and has distinct effects on organ size in hypophysectomized rats.

Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation

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Overexpression of Escherichia coli oxidoreductases increases recombinant insulin-like growth factor-I accumulation.

Isolation of the human insulin-like growth factor genes: insulin-like growth factor II and insulin genes are contiguous.

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