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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
【摘要】 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。
【Abstract】 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.
【Key words】 interleukin-2; pseudomonasexptoxin; fusionprotein; purification; renaturation;
- 【文献出处】 第一军医大学学报 ,Journal of First Military Medical University , 编辑部邮箱 ,2002年03期
- 【分类号】R392.11
- 【被引频次】7
- 【下载频次】157