[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. CONCLUSION 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.