中文摘要：

线粒体的呼吸耗氧偶联着ATP的合成,而位于线粒体内膜上的跨膜蛋白解偶联蛋白(uncoupling protein,UCP)能够破坏这种偶联关系.在大肠杆菌中表达了有生物活性的鼠源解偶联蛋白1(rUCP1).重组rUCP1的表达导致大肠杆菌宿主细胞生长变慢;在电子显微镜下观察免疫标记的结果显示,重组rUCP1主要表达在细菌膜上;同时将rUCP1重构到脂质体中也能够测到质子转运活性.这些结果说明,真核生物UCP1能够在原核生物中表达出有生物活性的形式,且能纯化得到足量的rUCP1蛋白用于进一步的结构生物学研究.

英文摘要：

Mitochondrial respiratory oxidation is coupled with ATP synthesis. This coupling process can be broken by uncoupling protein (UCP), an integral membrane protein at mitochondrial inner membrane. Here, active rat UCP1 (rUCP1) was expressed in E. coli. Expression of rUCP1 can lower host’s growth rate. Immuno-electron microscopy proved expressed rUCP1 was mainly located on membrane. Purified rUCP1 was reconstituted into liposome and exhibited proton translocation activity. These results revealed eukaryotic UCP1...