重组人白细胞介素2-绿脓杆菌外毒素融合蛋白的纯化及复性

Purification and renaturation of recombinant human interleukin-2-pseudomonas exotoxin(IL2-PE66 4Glu )fusion protein

目的探讨该所发明的新方法对重组人白细胞介素2-绿脓杆菌外毒素(IL2-PE664Glu)融合蛋白进行纯化与复性的效果。方法采用该所发明的新方法提纯包涵体,包涵体复性后,样品经DEAE-SepharoseFF离子交换层析,获得融合蛋白纯品。结果获得的具有生物学活性的融合蛋白纯度达到95%,复性回收率为80%。结论此包涵体分离纯化技术简便、实用,可为中试研究和规模化生产提供基础。

Objective To evaluatetheeffectof a novelapproachfor purificationand renaturationof recombinanthuman interleukin-2-pseudomonasexotoxin(IL2-PE66 4Glu )fusionprotein.Methods A novelpurificationmethodestablishedin our laboratorywas adoptedfor thepurificationof theinclusionbody,andafterrenaturation,recombinanthumanIL2-PE66 4Glu fusionproteinwas purifiedby DEAE-SepharoseFFion-exchangechromatography.Results Thepurityof thefusionprotein thatretainitsbiologicalactivitywasas highas95%,anda recoveryrateover80%of therefoldedIL2-PE66 4Glu fusionprotein was achieved.Conclusion The purificationand refoldingmethodfor inclusionbodyadoptedin thisstudyis simpleand practical,whichlaysthefoundationfora large-scaleproductionof thefusionprotein.