摘要
本文对大肠杆菌表达重组人白细胞介素－２（ｒＩＬ－２）进行了纯化研究。从ｒＩＬ－２菌株发酵后的包含体中，采用ＳｅｐｈａｃｒｙｌＳ－２００和ＤＥＡＥ－纤维素两种柱层析法纯化了ｒＩＬ－２，其比活性达４．１×１０￣６Ｕ／ｍｇ蛋白，回收率为３５％，提纯倍数为１９．５。
he purification of recombinant interleukin-2(rIL-2)expressed in E coli was stud-ied. The recombinant human interleukin-2 produced from inelusion bodies in E coli waspurified, by using column chromatography successively with Sephacryl S-200 and DEAE-cellulose. the specific activity was about 4.1×10 U/mg,the yield 35% and the purifiedfelds 19. 5.
