Production of a soluble and active MBP-scFv fusion: Favorable effect of the leaky tolR strain

被引：13

作者：

Chames, P ^{[1
]}

Fieschi, J ^{[1
]}

Baty, D ^{[1
]}

机构：

[1] CNRS,UPR 9027,LAB INGN & DYNAM SYST MEMBRANAIRES,INST BIOL STRUCT & MICROBIOL,F-13402 MARSEILLE 20,FRANCE

来源：

FEBS LETTERS | 1997年 / 405卷 / 02期

关键词：

secretion; aggregation; inclusion body; antibody; anti-cortisol; steroid;

D O I：

10.1016/S0014-5793(97)00194-4

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：

The 6D6 anti-cortisol scFv was prepared as fusion protein with maltose-binding protein (MBP) to increase the amount of soluble product. This fusion was almost completely insoluble when produced in a wild-type strain of Escherichia coli. However, when MBP-scFv fusion was produced in a tolR leaky strain, it was secreted into the culture medium as an active, soluble protein. Production of recombinant proteins in the tolR strain greatly enhances the recovery of active protein and may be a useful system to produce MBP fusion proteins that would normally aggregate when produced in wild-type bacterial strains. (C) 1997 Federation of European Biochemical Societies.

引用

页码：224 / 228

页数：5

共 30 条

[1] INVIVO DEGRADATION OF SECRETED FUSION PROTEINS BY THE ESCHERICHIA-COLI OUTER-MEMBRANE PROTEASE OMPT [J].