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.
出处
《药物生物技术》
CAS
CSCD
2006年第1期9-13,共5页
Pharmaceutical Biotechnology
