摘要
利用高分辨的１Ｈ核磁共振技术研究了 Ｃａ２＋对钙调蛋白（ＣａＭ）分子构象的影响以及酸枣仁皂甙 Ａ与 ＣａＭ的作用机制。研究结果表明；随着 Ｃａ２＋的加入． ＣａＭ分子的构象处于不断的变化之中。前两个Ｃａ２＋的加入主要结合在ＣａＭ的第Ⅲ，ⅣＣａ２＋结合位点（Ｃ结构域）上，后两个Ｃａ２＋的加入，则主要结合在ＣａＭ分子的第Ⅰ，Ⅱ Ｃａ２＋结合位点（Ｎ结构域〕上：酸枣仁皂甙 Ａ在 ＣａＭ上也有两类结合位点，一类是位于 ＣａＭ分子 Ｎ结构域上，只能结合一个药物分子的高亲合点；另一类是位于ＣａＭ分子Ｃ结构域上的至少能结合两个药物分子的低亲合点。
The effect on the conformation of calmodulin (CaM) when Ca2+ 's were added and the interactive mechanism between jujuboside A and calmodulin were studied using 400 MHz NMR spectroscopy. The results show that the conformation of calmodulin varies with adding Ca2+ into CaM, the first and second Ca2+ mainly entered into and bound in Ⅲ anb Ⅳ binding sites on CaM (C binding sites), but the last two Ca2+ mainly bound in Ⅰ and Ⅱ binding sites on CaM (N binding sites). There are two binding sites on CaM for jujuboside A. One is in N binding sites on CaM, where only one jujuboside A can be bound specifically, the other is in C binding sites on CaM, where at least two drug molecule can be bound nonspecifically.
出处
《清华大学学报（自然科学版）》
EI
CAS
CSCD
北大核心
1990年第6期46-52,共7页
Journal of Tsinghua University(Science and Technology)
基金
国家自然科学基金
