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

被引：39

作者：

Humphreys, DP

Weir, N

Lawson, A

Mountain, A

Lund, PA

机构：

[1] UNIV BIRMINGHAM,SCH BIOL SCI,BIRMINGHAM B15 2TT,W MIDLANDS,ENGLAND

[2] CELLTECH THERAPEUT LTD,SLOUGH SL1 4EN,BERKS,ENGLAND

来源：

FEBS LETTERS | 1996年 / 380卷 / 1-2期

关键词：

protein disulphide isomerase; antibody fragment; E-coli periplasm; protein folding;

D O I：

10.1016/0014-5793(96)00028-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 Fab' fragment in the periplasm of E. coli.

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页码：194 / 197

页数：4

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