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利用非抗体亲和层析，对白细胞介素－２基因在质粒ｐＭＡＬ－ｃＲ１中形成的克隆子表达的融合蛋白，进行分离纯化；并经特异性酶ｆａｃｔｏｒＸａ酶切，分离，得到纯度高达９８％的白细胞介素－２蛋白，收率为６９．７％，其比活为１０５Ｕ／ｍｇ。
The non-antibody affinity chromatography was used to isolate and purify the fusion protein expressed by the cloned subunit of interleukin-2 gene in plasmid pMAL-cR1. The recombinant protein was digested with specific enzyme factorXa, and the purity was 98% Of interleukin-2 protein in a yield of 69.7% with a specific activity of 105 U / mg.