【摘 要】
：
目的:为探索乙酰胆碱酯酶(AChE)活性中心狭隙与其水解底物高效性相适应的可能机制,研究胆碱类底物对AChE四聚体(AChE G4)亚分子结构的影响.方法:冰浴超声法制备磷脂膜,囊泡融
【机 构】
：
军事医学科学院毒物药物研究所,国家生物医学分析中心
【基金项目】
：
国家重点基础研究发展规划(973计划);国家高技术研究发展计划(863计划);北京市科学技术委员会重点计划
论文部分内容阅读
目的:为探索乙酰胆碱酯酶(AChE)活性中心狭隙与其水解底物高效性相适应的可能机制,研究胆碱类底物对AChE四聚体(AChE G4)亚分子结构的影响.方法:冰浴超声法制备磷脂膜,囊泡融合技术将AChE重组到以云母为支撑的磷脂膜上,原子力显微技术(AFM)观察AChE分别与乙酰胆碱(ACh)和丁酰胆碱(BCh)作用前后的亚分子结构.结果:单个AChE G4颗粒是表面光滑、中间突出的椭圆形结构,亚基排列紧密,平均大小为[(89±7)nm×(68±9)nm×(6±3)nm,长×宽×高,n=100].与底物反应后,可清楚地看到亚基排列松散,酶蛋白是由4个亚基组成,亚基之间形成一个无阻碍空间,这与X线晶体学和分子动力学研究结果相一致.与S-ACh反应后,单个AChE G4颗粒平均大小为[(104±7)nm×(91±5)nm×(8±2)nm,长×宽×高,n=100],无阻碍空间大小为[(60±5)nm×(51±9)nm,长×宽,n=30];与S-BCh反应后,酶的大小为[(100±5)nm×(87±6)nm×(7±3)nm,长×宽×高,n=100],无阻碍空间大小为[(38±4)nm×(35±2)nm,长×宽,n=30].结论:胆碱类底物对AChE G4亚分子结构具有明显影响,酶亚分子结构变化与其水解底物的高效性是一致的.
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