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

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Title
Simple purification of Escherichia coli-derived recombinant human interleukin-2 expressed with N-terminus fusion of glucagon
Author(s)
Hye Soon Won; Jee Won Lee; In Ho Kim; Young Hoon Park
Bibliographic Citation
Biotechnology and Bioprocess Engineering, vol. 5, no. 1, pp. 13-16
Publication Year
2000
Abstract
Simple procedures have been devised for purifying recombinant human interleukin-2 (hIL-2), which was expressed in Escherichia 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→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.
Keyword
human interleukin-2glucagonN-terminus fusionpurification process
ISSN
1226-8372
Publisher
Springer
DOI
http://dx.doi.org/10.1007/BF02932346
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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