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
Authors
Colleges, School and Institutes
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.
Details
Original language | English |
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Pages (from-to) | 194-7 |
Number of pages | 4 |
Journal | FEBS Letters |
Volume | 380 |
Issue number | 1-2 |
Publication status | Published - 12 Feb 1996 |
Keywords
- 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