A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Expression of a synthetic gene for human interleukin-4 in E. coli cells. Preparation of a biologically active protein
Tekijät: Batchikova NV, Kulagina MA, Lutsenko SV, Smirnov VA, Kanevskiĭ VIu, Riazanova LA, Nazimov IV, Sonina NV, Siniagina EA, Azhaev AV.
Kustannuspaikka: http://www.maik.rssi.ru/cgi-perl/journal.pl?lang=eng&name=biokhim&page=main
Julkaisuvuosi: 1992
Lehti:: Bioorganicheskaya Khimiya / Russian Journal of Bioorganic Chemistry
Artikkelin numero: pp. 660-670
Vuosikerta: 18
Numero: 5
Aloitussivu: 660
Lopetussivu: 670
Sivujen määrä: 11
Tiivistelmä
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.
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