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

D P Humphreys; N Weir; A Lawson; A Mountain; P A Lund

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

D P Humphreys, N Weir, A Lawson, A Mountain, P A Lund

Biosciences

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

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.

Original language	English
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

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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.",

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",

author = "Humphreys, {D P} and N Weir and A Lawson and A Mountain and Lund, {P A}",

year = "1996",

month = feb,

day = "12",

language = "English",

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pages = "194--7",

journal = "FEBS Letters",

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T1 - Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli

AU - Humphreys, D P

AU - Weir, N

AU - Lawson, A

AU - Mountain, A

AU - Lund, P A

PY - 1996/2/12

Y1 - 1996/2/12

N2 - 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.

AB - 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.

KW - Immunoglobulin Fab Fragments

KW - Antibodies, Monoclonal

KW - Protein Disulfide-Isomerases

KW - Humans

KW - Protein Folding

KW - Molecular Sequence Data

KW - Gene Expression

KW - Escherichia coli

KW - Recombinant Fusion Proteins

KW - Isomerases

KW - Amino Acid Sequence

M3 - Article

C2 - 8603736

SN - 0014-5793

VL - 380

SP - 194

EP - 197

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

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

Abstract

Keywords

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