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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antibodies, Monoclonal / biosynthesis*
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Escherichia coli / metabolism*
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Gene Expression
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Humans
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Immunoglobulin Fab Fragments / biosynthesis*
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Isomerases / biosynthesis*
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Isomerases / chemistry
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Molecular Sequence Data
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Protein Disulfide-Isomerases
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Protein Folding
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / chemistry
Substances
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Antibodies, Monoclonal
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Immunoglobulin Fab Fragments
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Recombinant Fusion Proteins
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Isomerases
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Protein Disulfide-Isomerases