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《China Biotechnology》 2009-01
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Efficient Expression and Purification Technique of a Mutant of Human Interleukin 2

LIU Ming-jun1 WANG Bin2 SONG Xu-xia2 QIAN Dong-meng2(1 Department of Clinical Immunologic Laboratory,Affiliated Hospital of Qingdao University Medical College,Qingdao 266003,China)(2 Key Laboratory of Medicine and Biotechnology,Qingdao University Medical College,Qingdao 266021,China)  
Mutants of recombinant hIL-2(rhIL-2),generated by using site-directed mutagenesis strategy,can increase anti-tumor activity and decrease toxicity.A mutant of hIL-2(MhIL-2) in which Asn88 was substituted by Arg88 was generated by using the strategy.To reduce the undesirable formation of inclusion body and maximize the yield of soluble MhIL-2 fusion protein,a protocol for the expression of soluble MhIL-2 fusion protein was adapted.Our results have indicated that soluble form of the MhIL-2 fusion protein is expressed from E.coli.Moreover,it also has facilitated purification of the MhIL-2.SDS-PAGE analysis revealed that the MhIL-2 protein was efficiently purified to 95% purity by the combination of nickel ion Chelating column chromatography,Desalting column chromatography,thrombin cleavage and Superdex 75 gel filtration column chromatography.Proliferation assay of T lymphocyte of purified MhIL-2 showed that the biological activity of MhIL-2 was higher than that of standard hIL-2 in vitro.This work not only describes an efficient preparation strategy of MhIL-2,but also introduces a highly active MhIL-2 that may have important clinical applicability.
【Fund】: 山东省自然科学基金资助项目(E99C02)
【CateGory Index】: Q786
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