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

FEBS Letters

Humphreys, David P.²  Weir, Neil¹  Mountain, Andrew¹  Lawson, Alastair¹  Lund, Peter A.² 

[1] Celltech Therapeutics Ltd., 216 Bath Road, Slough, Berkshire SLI 4EN, UK;School of Biological Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK

关键词: Protein disulphide isomerase;    Antibody fragment;    E. coli periplasm;    Protein folding;    Carb;    carbenicillin;    Cm;    chloramphenicol;    Fab′;    antibody fragment with hinge containing the variable and first constant domains of both heavy and light chain;    FCS;    foetal calf serum (heat inactivated);    IAA;    3-β-indole acrylic acid;    IPTG;    isopropyl β-d-thiogalactopyranoside;    PBS;    phosphate buffered saline;    PDI;    protein disulphide isomerase;    PPIase;    peptidyl-prolyl-cis-trans-isomerase;    TMB;    3;    3′;    5;    5′-tetramethylbenzidine;    Tween-20;    polyoxyethylenesorbitan monolaurate;   

DOI  :  10.1016/0014-5793(96)00028-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Gab′ fragment in the periplasm of E. coli.

【 授权许可】

Unknown