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작성일 : 12-07-17 17:37

(2007) Proteome analysis of recombinant Escherichia coli producing human glucagon-like peptide-1.

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http://www.sciencedirect.com/science/article/pii/S1570023206007604 [1134]

Proteome analysis of recombinant Escherichia coli producing human glucagon-like peptide-1.

Dae-Hee Lee, Sung-Gun Kim, Yong-Cheol Park, Soo-Wan Nam, Kelvin H. Lee and Jin-Ho Seo*
Journal of Chromatography B 849(1-2): 323-330. 2007.04.15.
(SCI I/F:2.888)

The proteomic response of recombinantEscherichiacoliproducinghumanglucagon-likepeptide-1 was analyzed by two-dimensional gel electrophoresis. Protein spots in two-dimensional gel could be identified by using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and their expression profiles were compared with those of nonproducing cells. Thirty-five intracellular proteins exhibited differential expression levels between the production and control strains. These changes reflected physiological responses to heterologous peptide production in recombinantE. coli. Specifically, physiological changes included the down-regulation of proteins involved in the central carbon metabolism, biosynthesis of cellular building blocks and peptides, and up-regulation of cell protection proteins and some sugar transport proteins. This comprehensive analysis would provide useful information for understanding physiological alterations to heterologous peptide production and for designing efficient metabolic engineering strategies for the production of recombinantpeptides in E. coli.

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