The expression of biologically active human p53 inLeishmaniacells: a novel eukaryotic system to produce recombinant proteins

The expression of biologically active human p53 in Leishmania cells: a novel eukaryotic system to produce recombinant proteins.

We have investigated the use of Leishmania cells as a novel eukaryotic expression system for the production of recombinant protein. These cells are easy to maintain, requiring no CO2 incubator or shaker, and can be grown in standard tissue culture media. Leishmania cells can be readily transfected with plasmid DNA by electroporation and transformants selected with antibiotic resistance. Recent ...

Expression of Biologically Active Recombinant B-Domain-Deleted Human Factor VIII in Mammalian Cells

The Over-Expression of Biologically Active Human Growth Hormone in a T5-Based System in Escherichia coli, Studying Temperature Effect

We studied the expression of human growth hormone (hGH) in E. coli under a bacteriophage T5-base promoter in a pQE30 expression vector. For an efficient expression of hGH cDNA, a number of codons at the hGH N-terminal coding region were altered based on the E. coli major codons. An over-expression of hGH in the bacteria, carrying the recombinant plasmids, was observed at 37°C in the presence of...

Purification of Large Quantities of Biologically Active Recombinant Human Growth Hormone

Production and purification of human growth hormone using a simple method was studied in two recombinantEscherichia coli, D7-5 and C27-2 strains. The r-hGH was expressed in the form of inclusion body in a batchfermentation process and purified to 99% purity using a procedure based on acid precipitation of the hostderived proteins and other impurities. The effect of the pH and ...

A Novel Vector for Expression/Secretion of Properly Folded Eukaryotic Proteins: a Comparative Study on Cytoplasmic and Periplasmic Expression of Human Epidermal Growth Factor in E. coli

Expression of eukaryotic proteins in E. coli often results in their aggregation. Proper folding and solubility of therapeutical proteins are the pre-requisite for their bioactivity. This is not achieved in cytoplasmic expression in E. coli because of the absence of disulfide bonds formation. A novel expression/secretion vector was constructed which exploited β-lactamase signal sequence to trans...