中文摘要：

帕金森病（Parkinson’s disease，PD）涉及两种蛋白——α-synuclein蛋白（SNCP）与14-3-3蛋白。通过重组，将这两种蛋白在大肠杆菌DH5α中表达，通过谷胱甘肽-Sepharose 4B亲和层析将其纯化，得到GST-14-3-3蛋白；利用凝血酶对纯化的融合蛋白GST-SNCP切割，再经谷胱甘肽-Sepharose 4B亲和层析获得SNCP．通过免疫共沉淀、GST pull down和ELISA等技术，证明SNCP能够与14-3-3蛋白结合；为了进一步证明SNCP也与在脑组织中的天然14-3-3蛋白发生作用，利用His pull down方法进行实验．结果证明，SNCP能够和脑组织中的14-3-3蛋白发生相互作用．这些结果从分子水平提供了SNCP与14-3-3蛋白相互作用的实验证据，为进一步了解SNCP的结构和功能，及其在中枢神经系统退行性疾病的作用提供了必要的实验基础．

英文摘要：

Recombinant α-synuclein protein （SNCP） and 14-3-3 protein, two proteins implicated in Parkinson＇ s disease （PD）, were expressed in E. coli DH 5α and purified by glutathione-Sepharose-4B. Purified GST-14-3-3 protein and SNCP were obtained by cleavage with thrombin. To investigate the interaction between SNCP and 14-3-3 protein, immuno-precipitation, GST pull-down and ELISA tests were used. The results showed that the purified full length SNCP interacted with 14-3-3 protein. The possible interaction between native protein extracts from brain tissues was observed. Further His pull-down experiments verified evidences of molecular interaction between SNCP and endogenously expressed 14-3-3 proteins. These results propose reliable experimenta data for the molecular interaction of SNCP with 14-3-3 protein in vivo, and provide experimental foundation for further study of SNCP＇ s biological functions and pathogenesis of neurodegenerative disorders.