Co‐expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab′ fragment expressed inEscherichia coli

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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 Gab′ fragment in the periplasm of E. coli

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