Simple Purification of Escherichia coli-Derived Recombinant Human Interleukin-2 Expressed with N-terminus Fusion of Glucagon

  • Won Hye-Soon (Chemical Engineering Department, Chungnam National University) ;
  • Lee Jeewon (Biochemical Process Engineering R.U., Korea Research Institute of Bioscience and Biotechnology (KRIBB)) ;
  • Kim In-Ho (Chemical Engineering Department, Chungnam National University) ;
  • Park Young-Hoon (Biochemical Process Engineering R.U., Korea Research Institute of Bioscience and Biotechnology (KRIBB))
  • Published : 2000.01.01


Simple procedures have been devised for purifying recombinant human interleukin-2 (hIL-2), which was expressed in Escberichia coli using sequences of glucagon molecules and enterokinase cleavage site as an N-terminus fusion partner. The insoluble aggregates of recombinant fusion protein produced in E. coli cytoplasm were easily dissolved by simple alkaline pH shift $(8\rightarrow12\rightarrow8)$. Following enterokinase cleavage, the recombinant hIL-2 was finally purified by one-step reversed-phase HPLC with high purity. The ease and high efficiency of this simple purification process seem to mainly result from the role of used glucagon fusion partner, which could be applied to the production of other therapeutically important proteins.


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