hVEGF165 Expression in Escherichia coli Conserves Its Biological Function  

作　　者：Gabajova Blanka Valkova Danka Bohac Andrej Kovacova Elena Moravcik Roman Zeman Michal 

机构地区：[1]Department of Organic Chemistry, FNS Comenius University, Bratislava 84215, Slovak Republic [2]Department of Animal Physiology and Ethology, FNS Comenius University, Bratislava 84215, Slovak Republic

出　　处：《Journal of Chemistry and Chemical Engineering》2012年第8期738-743,共6页化学与化工（英文版）

摘　　要：The paper describes the expression of human protein VEGF165 in Escherichia coli and its purification. This growth factor isoform contains exon 7, which is essential for binding to extracellular domain of VEGF receptor 2, located on endothelial cells lining the surface of blood vessels. This binding stimulates the cascade of downstream signalling events leading to process known as angiogenesis, hVEGF165 overexpressed with His-tag in BL21 E. coli cells forms inclusion bodies （insoluble protein）, so the research found the procedure for its solubilization and purification on a Nickel based affinity chromatography. Although this eukaryotic signal protein needs posttranslational processing for its full function as a homodimer, author verified the biological activity of our hVEGF165 protein, obtained as monomer, by wound healing test.

关 键 词：VEGFI65 endothelial cells HYPOXIA ANGIOGENESIS inclusion bodies protein purification wound healing test. 

分 类 号：Q55[生物学—生物化学] Q786