论文部分内容阅读
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。
In this paper, recombinant human interleukin-2 (rIL-2) expressed in Escherichia coli was purified. The rIL-2 was purified from the inclusion body of rIL-2 strain after fermentation by Sephacryl S-200 and DEAE-cellulose. The specific activity of rIL-2 was 4.1 × 10 ~ 6 U / mg protein. The recovery rate 35%, purification factor of 19.5.