Simple purification ofEscherichia coli-derived recombinant human interleukin-2 expressed with N-terminus fusion of glucagon |
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Authors: | Hye-Soon Won Jeewon Lee In-Ho Kim Young-Hoon Park |
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Institution: | (1) Chemical Engineering Department, Chungnam National University, 305-764 Taejon, Korea;(2) Biochemical Process Engineering R.U., Korea Research Institute of Bioscience and Biotechnology (KRIBB), Yusong, P.O. Box 115, 305-600 Taejon, Korea |
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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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Keywords: | human interleukin-2 glucagon N-terminus fusion purification process |
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