带信号肽DsbA-胸腺素α_1融合蛋白的表达及其分离纯化  

The expression and purification of DsbA-Tα_1 fusion protein with signal peptide

作　　者：郑小玲[1] 林陈水[1] 倪建良[1] 夏楠[1] 

机构地区：[1]浙江工业大学药学院,浙江杭州310032

出　　处：《浙江工业大学学报》2007年第6期613-616,共4页Journal of Zhejiang University of Technology

基　　金：浙江省科技厅资助项目(2005C33031)

摘　　要：以构建好的人胸腺素α1基因工程菌为研究材料,研究影响DsbA-胸腺素α1融合蛋白分泌效率的因素,优化信号肽酶表达得到阻遏的培养条件,获得含带信号肽DsbA-胸腺素α1融合蛋白的菌体,破碎细胞后利用疏水层析与Ni2+螯合亲和层析进行目标蛋白分离纯化,获得较高纯度底物蛋白(信号肽DsbA-胸腺素α1融合蛋白,其分子量约为34 kD),为进一步研究及分离纯化DsbA信号肽酶创造条件.Using the constructed Thymosin alpha1 strain as a material,influence factors on secretion of DsbA-Thymosin alphal fusion protein was studied.The incubation condition of preventing signal peptidase expression was optimized,and the cells contained DsbA-Tα1 fusion protein with signal peptide was obtained.After the ultrasonic broken-up and purified by hydrophobic interaction chromatography and nickel affinity chromatography,the high purification degree protein（the signal peptide-DsbA-Tα1 fusion protein,molecular weight about 34 kD） was obtained.These create the possibility for further separation,purification and studies of DsbA signal peptidase.

关 键 词：融合蛋白 信号肽 疏水层析 镍离子亲和层析 

分 类 号：TQ936.21[化学工程]