中文摘要：

[目的]获得高纯度的谷胱甘肽硫转移酶／抗癫痫肽（GST—AEP）融合蛋白。[方法]异丙基-β-D硫代半乳糖苷（IPTG）诱导重组大肠杆菌DH5α表达GST—AEP融合蛋白，融合蛋白包涵体经过洗涤、变性、复性后，通过12％SDS-PAGE凝胶电泳，考马斯亮蓝染色，凝胶薄层扫描检测其纯度，透析管进一步纯化蛋白，BCA法定量。[结果]从融合蛋白包涵体中获得了纯度达90％以上的目的蛋白，定量约0．163μg／μl。[结论]建立了有效纯化融合蛋白包涵体GST—AEP的方法，为对AEP进一步的相关研究奠定了基础。

英文摘要：

[Aim] To gain the fusion protein purified GST-AEP. [Methods] The protein GST-AEP was expressed in E. Coli-DH5α as a fusion protein induced by IPTG. The protein was a kind of inclusion body. The purifying and refolding to inclusion body were optimized. The purity of GST-AEP was identified by 12% SDS-PAGE and thin-layer scanning analysis. The quantitation of the fusion protein GST-AEP was done with BCA Protein Assay. [Results] Purity of GST-AEP was higher than 90% and concentration was about 0. 163μg/μl. [Conclusion] The fusion protein was highly purified and the method of fusion protein purification from the inclusion body was developed,which was the basis for further study on AEP.