Protein mobility in the cytoplasm of Escherichia coli.

Soluble Expression of Recombinant Nerve Growth Factor in Cytoplasm of Escherichia coli

Background: Pivotal roles of Nerve growth factor (NGF) in the development and survival of both neuronal and non-neuronal cells indicate its potential for the treatment of neurodegenerative diseases. However, investigation of NGF deficits in different diseases requires the availability of properly folded human b-NGF. In previous studies bacterial expression of hNGF demonstrated the feasibility o...

CONSTRUCTION OF RECOMBINANT PLASMIDS FOR PERIPLASMIC EXPRESSION OF HUMAN GROWTH HORMONE IN ESCHERICHIA COLI UNDER T7 AND LAC PROMOTERS

In order to study the periplasmic expression of human growth hormone (hGH) in Escherichia coli, the related cDNA was inserted in two expression plasmids carrying pelB signal peptide, one with lac bacterial promoter and the other with a bacteriophage T7-based promoter. The recombinant plasmids were moved to TG1 and BL21 strains of E. coli, respectively. To induce the expression systems, IPTG and...

Expression of Recombinant Protein B Subunit Pili from Vibrio Cholera

Background & Aims: Vibrio cholerae is a gram-negative bacterial pathogen that causes cholera disease. Following ingestion by a host and entry into the upper intestine, V. cholera colonizes and begins to emit enterotoxin. One of the most pathogenic factors of Vibrio cholera is toxin-coregulated pili (TCP). ToxinCoregulated pili is as the primary factor requiered for the colonization and insisten...

Molecular Cloning and Characterization of a Lipase from an Indigenous Bacillus pumilus

Cloning and sequencing of a lipase gene from an indigenous Bacillus pumilus, strain F3, revealed an open-reading frame of 648 nucleotides predicted to encode a protein of 215 residues. Sequence analysis showed that F3 lipase contained a signal peptide composed of 34 amino acids with an H domain of 18 residues. A tat-like motif was found in the signal peptide similar to some other Bacillus pumil...

Overexpression of Full-Length Core Protein of Hepatitis C Virus by Escherichia coli Cultivated in Stirred Tank Fermentor

The mature core protein of the Hepatitis C virus (HCVC173) carrying pelB as a signal peptide (PelB::core) was overexpressed in Escherichia coli as 18% and 23.3% of the host’s total protein, in flask and fermentor cultivation, respectively. A final specific yield of 25 ± 1 mg HCVC173/g dry cell weight and an overallproductivity of 51±1 mg HCVC173/l/h were obtained in the stirred-tank ferme...

Cloning and Expression of the Coat Protein Gene of Barley Yellow Dwarf Virus-PAV in Escherichia coli