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pMAL-c5x将 rhIL-2与MBP融合,在大肠杆菌BL21(DE3)中诱导MBP-rhIL2的表达.接着用Amylose树脂将MBP-rhIL2纯化,最后利用Factor Xa蛋白酶将rhIL-2从融合蛋白中释放.结果显示:MBP-rhIL2以可溶形式表达;Factor Xa成功将rhIL-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 amy-lose 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 ×106IU/mg.
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