[Using process of refolding the protein to obtain recombinant human interleukin-1 receptor antagonist].
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.
Li
Shugang
S
College of Bioengineering of Chongqing University, Chongqing 400044, China.
Deng
Xiaoyan
X
Zhao
Hong
H
Huang
Xiudong
X
Yu
Tinghe
T
Cheng
Yong
Y
Dan
Guoping
G
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006801:Humans; D002479:Inclusion Bodies / Q000378:metabolism*; D053590:Interleukin 1 Receptor Antagonist Protein / Q000096:biosynthesis* / Q000235:genetics; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification
D053590:Interleukin 1 Receptor Antagonist Protein; D011994:Recombinant Proteins