Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli
Research output: Contribution to journal › Article › peer-review
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.
|Number of pages||4|
|Publication status||Published - 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