摘要
本文研究了铝与钙调蛋白相互作用的荧光光谱。实验证明,Al^3与CaM的结合所引起的构象变化与Ca^(2+)与CaM结合所引起的构象变化既有相同之处,也有不同之处。Al^(3+)在CaM分子上的结合有特异性结合与非特异性结合两种情况。其特异性结合位点可能为2—3个。钙调蛋白的非竞争性拮抗剂酸枣仁皂甙A(JuA)可以继续抑制已被Al^(3+)部分抑制的PDE-CaM的活力。
The interaction between aluminium and calmodulin has been studied with the fluorescence spectrometer. It has shown that the conformation changes due to the binding of Al^(3+) to CaM are different from those due to the binding of Ca^(2+) to CaM. There are two kinds of binding sites: specific and nonspecific binding sites in the binding of Al^(3+) to CaM molecules, sites are about 2—3 specific binding, Jujuboside A is an inhibitor of calmodulin, it can still inhibit the reaction of CaM-PDE system which has been inhibited by Al^(3+).
基金
国家自然科学基金
北京分子动态基金
稳态结构实验室开放基金
关键词
铝
荧光
光谱
调钙蛋白
Calmodulin
Aluminium
Fluorescence
