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 language | English |
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Pages (from-to) | 13-16 |
Number of pages | 4 |
Journal | Biotechnology and Bioprocess Engineering |
Volume | 5 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2000 |
Externally published | Yes |
Keywords
- Glucagon
- Human interleukin-2
- N-terminus fusion
- Purification process
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology
- Biomedical Engineering