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

Hye Soon Won, Jeewon Lee, In Ho Kim, Young Hoon Park

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)13-16
Number of pages4
JournalBiotechnology and Bioprocess Engineering
Volume5
Issue number1
Publication statusPublished - 2000
Externally publishedYes

Fingerprint

Enteropeptidase
Glucagon
Escherichia coli
Interleukin-2
Purification
Fusion reactions
Recombinant Fusion Proteins
Proteins
Cytoplasm
High Pressure Liquid Chromatography
Molecules

Keywords

  • Glucagon
  • Human interleukin-2
  • N-terminus fusion
  • Purification process

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Biomedical Engineering

Cite this

Simple purification of Escherichia coli-derived recombinant human interleukin-2 expressed with N-terminus fusion of glucagon. / Won, Hye Soon; Lee, Jeewon; Kim, In Ho; Park, Young Hoon.

In: Biotechnology and Bioprocess Engineering, Vol. 5, No. 1, 2000, p. 13-16.

Research output: Contribution to journalArticle

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