A1 Refereed original research article in a scientific journal
Expression of a synthetic gene for human interleukin-4 in E. coli cells. Preparation of a biologically active protein
Authors: Batchikova NV, Kulagina MA, Lutsenko SV, Smirnov VA, Kanevskiĭ VIu, Riazanova LA, Nazimov IV, Sonina NV, Siniagina EA, Azhaev AV.
Publishing place: http://www.maik.rssi.ru/cgi-perl/journal.pl?lang=eng&name=biokhim&page=main
Publication year: 1992
Journal:: Bioorganicheskaya Khimiya / Russian Journal of Bioorganic Chemistry
Article number: pp. 660-670
Volume: 18
Issue: 5
First page : 660
Last page: 670
Number of pages: 11
Abstract
Expression E. coli plasmid were constructed in which the human interleukin-4 (hIL4) synthetic gene is controlled by tac promoter. The expression level of the gene depends on the distance between RBS and the initial codon ATG, with the maximal production in case of the nine base pair distance. The recombinant protein, accumulated in the inclusion bodies, was solubilized, renaturated, and purified to homogeneous, biologically active preparation, the yield being 2 mg/g wet cells.
Expression E. coli plasmid were constructed in which the human interleukin-4 (hIL4) synthetic gene is controlled by tac promoter. The expression level of the gene depends on the distance between RBS and the initial codon ATG, with the maximal production in case of the nine base pair distance. The recombinant protein, accumulated in the inclusion bodies, was solubilized, renaturated, and purified to homogeneous, biologically active preparation, the yield being 2 mg/g wet cells.
UTU Research Portal