摘要
为探索白细胞介素-2在大肠杆菌中的可溶表达及其生物学活性,利用载体p MAL-c5x将rh IL-2与MBP融合,在大肠杆菌BL21(DE3)中诱导MBP-rh IL2的表达。接着用Amylose树脂将MBP-rh IL2纯化,最后利用Factor Xa蛋白酶将rh IL-2从融合蛋白中释放。结果显示:MBP-rh IL2以可溶形式表达;Factor Xa成功将rh IL-2从融合蛋白中释放出来;经生物学活性测定,其比活性为4.4×106IU/mg。
This work aims to explore the soluble expression and biological activity of interleukin-2;recombinant fusion protein MBP-rhIL2 was successfully expressed into soluble form in E.coli BL21(DE3).The purification of MBP-rhIL2 was conducted through amylose resin.The rhIL-2 was efficiently released by the cleavage of protease Factor Xa from the fusion protein.Bioactivity analysis showed the biological activity of purified rhIL-2 is 4.4×10 6 IU/mg.
作者
李冠英
李海红
徐士勋
潘晓雨
LI Guan-ying;LI Hai-hong;XU Shi-xun;PAN Xiao-yu(Shanghai Huaxin High Biotechnology Inc.,Shanghai 201206,China)
出处
《生物学杂志》
CAS
CSCD
北大核心
2018年第1期107-110,共4页
Journal of Biology
基金
上海张江国家自主创新示范区专项发展资金(201411-PD-JQ-C104-013)
关键词
白细胞介素-2
可溶表达
蛋白纯化
Interleukin-2
soluble expression
protein purification
