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作者采用７ｍｏｌ／Ｌ盐酸肌直接裂解重组人白细胞介素２（ｒｈＩＬ－２）工程菌，溶解包含体蛋白，利用疏水色谱、凝胶过滤、离子交换分离纯化ｒｈＩＬ－２，各步收率分别为１４０％，８５％，７０％。终产品比活性为１．９×１０￣６Ｕ／ｍｇ，经ＳＤＳ－ＰＡＧＥ鉴定为单一条带，得到高比活高纯度的ｒｈＩＬ－２．本方法利用疏水色谱既能分离又能促进ｒｈＩＬ－２复性的特点，克服了包含体蛋白较难溶解又易聚合的缺点，提高了ｒｈＩＬ－２活性，简化了实验步骤，用常压色谱使ｒｈＩＬ－２的大量纯化成为可能。
Using 7mol / L hydrochloric acid muscle, recombinant rhIL-2 engineered bacteria were directly lysed to dissolve the inclusion body proteins. RhIL-2 was purified and purified by hydrophobic chromatography, gel filtration and ion exchange. The yield of each step was 140%, 85%, 70%. The final product specific activity of 1.9 × 10 ~ 6U / mg, identified by SDS-PAGE as a single band, to obtain high specific activity and high purity rhIL-2. The method utilizes both hydrophobic chromatographic separation and refolding of rhIL-2, overcomes the shortcomings that the inclusion body protein is difficult to be dissolved and polymerizes, improves the activity of rhIL-2, simplifies the experimental procedure, A large number of rhIL-2 purification possible.