hVEGF165 Expression in Escherichia coli Conserves Its Biological Function

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

作者机构：Department of Organic Chemistry FNS Comenius University Bratislava 84215 Slovak Republic Department of Animal Physiology and Ethology FNS Comenius University Bratislava 84215 Slovak Republic 

出 版 物：《Journal of Chemistry and Chemical Engineering》 (化学与化工（英文版）)

年 卷 期：2012年第6卷第8期

页      面：738-743页

学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 09[农学] 071007[理学-遗传学] 0901[农学-作物学] 0836[工学-生物工程] 090102[农学-作物遗传育种] 

主　　题：大肠杆菌细胞 表达产物 生物活性 血管内皮生长因子受体 人类蛋白质 VEGF165 血管内皮细胞 信号蛋白 

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.