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

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Colleges, School and Institutes


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.


Original languageEnglish
Pages (from-to)194-7
Number of pages4
JournalFEBS Letters
Issue number1-2
Publication statusPublished - 12 Feb 1996


  • Immunoglobulin Fab Fragments, Antibodies, Monoclonal, Protein Disulfide-Isomerases, Humans, Protein Folding, Molecular Sequence Data, Gene Expression, Escherichia coli, Recombinant Fusion Proteins, Isomerases, Amino Acid Sequence