title: Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli.
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.
authors.affiliation: School of Biological Sciences, University of Birmingham, UK.
authors.forename: D P
authors.initials: DP
authors.lastname: Humphreys
authors.forename: N
authors.initials: N
authors.lastname: Weir
authors.forename: A
authors.initials: A
authors.lastname: Lawson
authors.forename: A
authors.initials: A
authors.lastname: Mountain
authors.forename: P A
authors.initials: PA
authors.lastname: Lund
mesh_terms: D000595:Amino Acid Sequence; D000911:Antibodies, Monoclonal / Q000096:biosynthesis*; D004926:Escherichia coli / Q000378:metabolism*; D015870:Gene Expression; D006801:Humans; D007140:Immunoglobulin Fab Fragments / Q000096:biosynthesis*; D007535:Isomerases / Q000096:biosynthesis* / Q000737:chemistry; D008969:Molecular Sequence Data; D019704:Protein Disulfide-Isomerases; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry
chemical_list: D000911:Antibodies, Monoclonal; D007140:Immunoglobulin Fab Fragments; D011993:Recombinant Fusion Proteins; D007535:Isomerases; D019704:Protein Disulfide-Isomerases