人重组IL6／IL2融合蛋白的变性、复性及纯化  

Purification and Renaturation of RecombinantFusion Protein IL6/IL2.

作　　者：赵春华[1] 凌世淦[1] 毛宁[1] 唐佩弦[1] 

机构地区：[1]北京军事医学科学院基础医学研究所

出　　处：《生物化学与生物物理进展》1994年第5期432-435,共4页Progress In Biochemistry and Biophysics

基　　金：国家青年"863"基金

摘　　要：经超声破碎，分离已表达ＣＨ９２５包涵体，较系统地研究变性剂浓度、融合蛋白浓度对蛋白折叠的影响．在还原型及氧化型谷胱甘肽复性条件下。The expressed CH925 was aggregated into in-clusion bodies (IB) in E. coli cytoplasm. TheIBs were isolated by centrifugation and sonica-tion. CH925 were.refolded and reoxidateo in aglutathione redox system following denatura-tion of the IBs in 7mol/L guanidine hydrochio-ride. The specificactivities of ILZ and IL6 as-sayed by CTLL-2 and 7TDl cell line were 2. 2× 10￣6U/mg and 2. 3 × 10￣8U/mg, respectively,following renaturation. The renatured CH925was chromatographed through DEAE-Sepharose 6B column and Sephacryl column.The active fractions were pooled and appliedto HPLC with reversedphase C-18 column.while CH925 was eluted through 10%-70%acetonitrile gradient. It showed oniy one pro-tein peak and SDS-PAGE confirmed that thepurified CH92O was almost homogeneous.

关 键 词：白细胞介素 重组 融合蛋白 变性 提纯 

分 类 号：R392－33[医药卫生—免疫学] Q510.3[医药卫生—基础医学]