Expression of the human erythrocyte glucose transporter in Escherichia coli.

Optimization of secretory expression of recombinant hGM-CSF in high cell density cultivation of recombinant Escherichia coli using Taguchi statistical method

Human granulocyte macrophage colony stimulating factor (hGM-CSF) has many therapeutic applications.In this study, in order to verify the purification process, the effect of carbon source, IPTG concentration andpost-induction time on the secretion of recombinant hGM-CSF into the culture medium by recombinantEscherichia coli during high cell density cultivation were evaluated by...

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 and Secretion of Human Granulocyte Macrophage-Colony Stimulating Factor Using Escherichia coli Enterotoxin I Signal Sequence

With the aim of the secretion of human granulocyte macrophage-colony stimulating factor (hGM-CSF) in Escherichia coli, hGM-CSF cDNA was fused in-frame next to the signal sequence of ST toxin (ST-I) of exteroxigenic E. coli, containing 53 or 19 amino acids of signal peptide. The fused STsig::hGM-CSF coding fragments were inserted into a T7-based expression plasmid. The recombinant plasmids were ...

Comparison of T7- and Lac-Based Systems for the Periplasmic Expression of Human Granulocyte Macrophage Colony Stimulating Factor in Escherichia coli

A COMPARATIVE STUDY BETWEEN EXPRESSION OF A SYNTHETIC GENE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR (hbFGF) AND ITS RELATED cDNA IN ESCHERICHIA COLI

The gene encoding the human basic fibroblast growth factor (hbFGF) has been already chemically-synthesized and cloned in pET-3a expression vector (Pasteur Institute of Iran). In the present study, we compared the level of expression of this synthetic hbFGF and its related cDNA in Escherichia coli. The pBR322-cDNA of hbFGF supplied by Dr. Seno (from Molecular Biology Dept, Okaido prefectural uni...