Using process of refolding the protein to obtain recombinant human interleukin-1 receptor antagonist / 生物医学工程学杂志
Journal of Biomedical Engineering
; (6): 1128-1132, 2007.
Article
in Zh
| WPRIM
| ID: wpr-230735
Responsible library:
WPRO
ABSTRACT
Recombinant human interleukin-1 receptor antagonist was expressed in E. coli as an insoluble inclusion body. The inclusion body was dissolved in the 8 M urea and then the solution was diluted untill the concentration of urea became 2 M. By ion exchange chromatography the protein in the solution of 2 M urea was refolded and purified. At last the purity of product is more than 95% and its bioactivity is more than 1 x 10(5) IU/mg while it has little endotoxin. Western-Blotting also indicates that recombinant protein can react with antibodies against anti-hIL-1ra.
Full text:
1
Index:
WPRIM
Main subject:
Recombinant Proteins
/
Inclusion Bodies
/
Protein Folding
/
Escherichia coli
/
Interleukin 1 Receptor Antagonist Protein
/
Genetics
/
Metabolism
Limits:
Humans
Language:
Zh
Journal:
Journal of Biomedical Engineering
Year:
2007
Type:
Article