A1 Refereed original research article in a scientific journal
Secretion of recombinant human epidermal growth factor into the periplasm in Escherichia coli cells
Authors: Batchikova NV, Al'tman IB, Lutsenko SV, Smirnov VA, Nazimov IV, Eshkind LG, Siniagina EA, Azhaev AV.
Publishing place: http://www.maik.rssi.ru/cgi-perl/journal.pl?lang=eng&name=biochem
Publication year: 1992
Journal:: Bioorganicheskaya Khimiya / Russian Journal of Bioorganic Chemistry
Journal acronym: Bioorg khim
Volume: 18
Issue: 6
First page : 766
Last page: 776
Abstract
Secretion vectors were constructed in which a synthetic gene of human epidermal growth factor (hEGF) joined with a gene coding for the leader peptide to one of the E. coli outer membrane major proteins (OmpF) is controlled by tac promoter. The increase of the hEGF yield was achieved by the multiplication of the gene copies. The hEGF in bacterial cells was secreted into periplasm. The recombinant protein was isolated by means of reverse phase chromatography as almost homogenous preparation (greater than 98%), the yield being 7 mg/l bacterial culture. The sequence of twenty-five N-terminal amino acid residues of the isolated hEGF coincided with that of the natural protein. The preparation proved to be biologically active.
Secretion vectors were constructed in which a synthetic gene of human epidermal growth factor (hEGF) joined with a gene coding for the leader peptide to one of the E. coli outer membrane major proteins (OmpF) is controlled by tac promoter. The increase of the hEGF yield was achieved by the multiplication of the gene copies. The hEGF in bacterial cells was secreted into periplasm. The recombinant protein was isolated by means of reverse phase chromatography as almost homogenous preparation (greater than 98%), the yield being 7 mg/l bacterial culture. The sequence of twenty-five N-terminal amino acid residues of the isolated hEGF coincided with that of the natural protein. The preparation proved to be biologically active.
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