Investigators from University of Southampton Release New Data on Intercellular Signaling Peptides and Proteins (Characterization and bioassay of post-translationally modified interferon alpha-2b expressed in Escherichia coli)
By a News Reporter-Staff News Editor at Biotech Week -- Research findings on Intercellular Signaling Peptides and Proteins are discussed in a new report. According to news reporting originating in Southampton, United Kingdom, by NewsRx journalists, research stated, "Examples of N-terminal acetylation are rare in prokaryotic systems, but in this study, we report one such example in which N-terminal Cys residue of recombinant human interferon alpha-2b produced in Escherichia coil is a favourite site for N-alpha-acetylation. The recombinant protein following Q-sepharose chromatography gave a single band on PAGE analysis."
The news reporters obtained a quote from the research from the University of Southampton, "However, on reverse phase HPLC the material separated into three peaks. These were characterized by mass spectrometric techniques as: (a) the direct translation product of the gene retaining the N-terminal methionine, (b) a species from which the methionyl residue had been removed by E. coli methionyl aminopeptidase to give the native interferon alpha-2b and © in which the N-terminal Cys residue of the latter contained an acetyl group. Tryptic digestion of interferon alpha-2b gave fragments linking Cys(1) to Cys(98) and Cys(29) to Cys(138), while that of N-alpha-acetyl-interferon alpha-2b gave the Cys(1)-Cys(98) fragment with an additional mass of 42 attributed to an acetylated N-terminal. Bioassay of the derivatives showed that N-alpha-acetyl-interferon alpha-2b had 10% of the activity of interferon alpha-2b."
According to the news reporters, the research concluded: "The results suggest that the lower activity derivative seen here in E. coli may also be produced when the protein is produced in yeast."
For more information on this research see: Characterization and bioassay of post-translationally modified interferon alpha-2b expressed in Escherichia coli. Journal of Biotechnology, 2014;184():11-16. Journal of Biotechnology can be contacted at: Elsevier Science Bv, PO Box 211, 1000 Ae Amsterdam, Netherlands. (Elsevier - www.elsevier.com; Journal of Biotechnology - www.elsevier.com/wps/product/cws_home/505515)
Our news correspondents report that additional information may be obtained by contacting F. Ahsan, University of Southampton, Center Biol Sci, Southampton SO17 1BJ, Hants, United Kingdom. Additional authors for this research include A. Arif, N. Mahmood, Q. Gardner, N. Rashid and M. Akhtar (see also Intercellular Signaling Peptides and Proteins).
Keywords for this news article include: Southampton, United Kingdom, Europe, Biological Factors, Cytokines, Enterobacteriaceae, Escherichia, Gammaproteobacteria, Intercellular Signaling Peptides and Proteins, Interferon Type I, Interferon-alpha, Interferons
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