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Simple purification ofEscherichia coli-derived recombinant human interleukin-2 expressed with N-terminus fusion of glucagon

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Abstract

Simple procedures have been devised for purifying recombinant human interleukin-2 (hIL-2), which was expressed inEscherichia coli using sequences of glucagon molecules and enterokinase cleavage site as an N-terminus fusion partner. The insoluble aggregates of recombinant fusion protein produced inE. coli cytoplasm were easily dissolved by simple alkaline pH shift (8→12→8). 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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Authors and Affiliations

  1. Chemical Engineering Department, Chungnam National University, 305-764, Taejon, Korea

    Hye-Soon Won & In-Ho Kim

  2. Biochemical Process Engineering R.U., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Yusong, P.O. Box 115, 305-600, Taejon, Korea

    Jeewon Lee & Young-Hoon Park

Authors
  1. Hye-Soon Won
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  2. Jeewon Lee
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  3. In-Ho Kim
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  4. Young-Hoon Park
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Correspondence to In-Ho Kim.

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Won, HS., Lee, J., Kim, IH. et al. Simple purification ofEscherichia coli-derived recombinant human interleukin-2 expressed with N-terminus fusion of glucagon. Biotechnol. Bioprocess Eng. 5, 13–16 (2000). https://doi.org/10.1007/BF02932346

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  • DOI: https://doi.org/10.1007/BF02932346

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