重组人血管内皮生长因子(hVEGF121)工程菌的发酵及表达产物的分离纯化  

Isolation and Purification of Recombinant Human Vascular Endothelial Growth Factor (hVEGF) Expressed in E.coli

作　　者：周红霞[1] 周梅仙[2] 廖忠平[1] 吴洁[1] 胡卓逸[1] 刘景晶[1] 

机构地区：[1]中国药科大学生命科学与技术学院微基因药物实验室,江苏南京210009 [2]南京晓庄学院生命科学系,江苏南京210017

出　　处：《药物生物技术》2006年第1期9-13,共5页Pharmaceutical Biotechnology

摘　　要：该研究优化了重组人血管内皮生长因子hVEGF121工程菌的发酵条件,考察乳糖诱导浓度和时间对目的蛋白表达量的影响。经乳糖诱导,目的蛋白以包涵体形式存在。通过菌体裂解、包涵体洗涤、裂解等初步纯化后,再经过DEAE-Cellulose离子交换柱纯化和复性,经SDS-PAGE分析显示得到电泳纯的hVEGF121。The expression condition of recombinant human vascular endothelial growth factor 121 in E. coli expression system is optimized in this paper. After being induced by 2% lactose for 6h, recombinant protein was expressed. Results showed that gene highly expressed its product in inclusion body. By denaturation, purification with DEAE-cellulose chromatography and renaturation, the inclusion body was purified. The purity of product was above 90% analyzed by SDS-PAGE. It can be concluded that the recombinant human VEGF121 was expressed and purified successfully.

关 键 词：血管内皮生长因子 表达 纯化 包涵体 

分 类 号：Q51[生物学—生物化学]