Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli

FEBS Letters
D P HumphreysP A Lund

Abstract

Secretion to the periplasm of Escherichia coli enables production of many eukaryotic extracellular proteins in a soluble form. The complex disulphide bond arrangement of such proteins is probably a major factor in determining the low yield of correctly folded product observed in many cases. Here we show that co-expression of human protein disulphide isomerase increased the yield of a monoclonal antibody Fab' fragment in the periplasm of E. coli.

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Citations

Oct 26, 2012·Molecular Biotechnology·Dmitrij HristodorovLars Linden
Feb 3, 1999·Annals of the New York Academy of Sciences·C C Wang
Nov 10, 2001·Annual Review of Biomedical Engineering·J Maynard, G Georgiou
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Oct 5, 2011·Protein Expression and Purification·Diane M RetallackLawrence Chew
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Nov 17, 2011·Protein Expression and Purification·Mehmet Berkmen
Sep 11, 2004·Biochemical and Biophysical Research Communications·Haiping ZhouKaiyu Yang
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Oct 2, 2014·Current Protocols in Molecular Biology·Na Ke, Mehmet Berkmen
Sep 30, 2021·Biotechnology and Bioengineering·Hirra HussainChristopher M Smales

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