In this study we investigate the effect of thioredoxin (Trx1) protein fusions in the production,
oxidation, and folding of single chain Fv (scFv) antibodies in the cytoplasm of Escherichia …

The production of a single-chain variable fragment (scFv) antibody against bovine
ribonuclease A in the cytoplasm of Escherichia coli trxB/gor double mutant was investigated …

Production of intracellular antibodies in Escherichia coli has been thought unlikely owing to
an inability to form stable disulfide bonds in the cytoplasm, a necessary step in the folding of …

Overproduction of recombinant proteins in Escherichia coli is often hampered by their failure
to fold correctly, leading to their accumulation within inclusion bodies. To overcome the …

The cytoplasmic expression of a functional antibody (Ab) fragment, containing the correct
intradomain disulfide bonds, was investigated in E. coli. We used a single-chain Fv (scFv) …

Single-chain Fv antibodies (scFv), a group of reconstructed molecules with several disulfide
bonds, are prone to aggregate as inclusion bodies, the insoluble species of natural proteins …

Background Disulfide bonds are the most common structural, post-translational modification
found in proteins. Antibodies contain up to 25 disulfide bonds depending on type, with scFv …

AIM: To study the influence of redox environment of Escherichia coli (E. coli) cytoplasm on
disulfide bond formation of recombinant proteins. METHODS: Bovine fibroblast growth factor …

Under physiological conditions, the Escherichia coli cytoplasm is maintained in a reduced
state that strongly disfavors the formation of stable disulfide bonds in proteins. However …

A recently developed E. coli thioredoxin (Trx) gene fusion expression system has
circumvented the difficulties associated with inclusion body formation. Although ample …