[Purification and renaturation of recombinant human interleukin-2-pseudomonas exotoxin (IL2-PE66(4GLU)) fusion protein].
OBJECTIVE
To evaluate the effect of a novel approach for purification and renaturation of recombinant human interleukin-2-pseudomonas exotoxin (IL2-PE66(4Glu)) fusion protein.


METHODS
A novel purification method established in our laboratory was adopted for the purification of the inclusion body, and after renaturation, recombinant human IL2-PE66(4Glu) fusion protein was purified by DEAE-Sepharose FF ion-exchange chromatography.


RESULTS
The purity of the fusion protein that retain its biological activity was as high as 95%, and a recovery rate over 80% of the refolded IL2-PE66(4Glu) fusion protein was achieved.


CONCLUSIONS
The purification and refolding method for inclusion body adopted in this study is simple and practical, which lays the foundation for a large-scale production of the fusion protein.
Hu
Zhi-Ming
ZM
Institute of Molecular Immunology, First Military Medical University, Guangzhou 510515, China. hzm@fimmu.edu.cn
Linlai
Xing-Mei
XM
Zhou
Ming-Qian
MQ
Chen
Ze-Hong
ZH
Wang
Xiao-Ning
XN
D000818:Animals; D002470:Cell Survival / Q000187:drug effects; D004591:Electrophoresis, Polyacrylamide Gel; D005098:Exotoxins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D006801:Humans; D007376:Interleukin-2 / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D020673:Protein Renaturation; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology
D005098:Exotoxins; D007376:Interleukin-2; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; C065698:interleukin 2-PE66(4Glu) protein, recombinant