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作 者:蔡小强[1] 潘逆娜[1] 郑忠亮[1] 邹国林[1]
出 处:《武汉大学学报(理学版)》2008年第4期443-446,共4页Journal of Wuhan University:Natural Science Edition
基 金:国家自然科学基金(30370366);高等学校博士学科点专项科研基金资助项目
摘 要:用IAsys光学生物传感器与荧光淬灭法研究了菲咯啉铜配合物与组蛋白H1的相互作用,得出了在25℃和pH 7.4条件下两者的结合常数和结合位点数.结果表明,菲咯啉铜配合物与组蛋白H1具有较强的相互作用,其结合常数数量级可达到105,两者相互作用时只有一个结合位点,菲咯啉铜配合物与组蛋白H1的结合常数是单独的菲咯啉配体的6倍.推测菲咯啉铜配合物在诱导细胞凋亡的过程中在与组蛋白H1结合处切割核小体上的DNA,从而产生凋亡所特有的DNA片段化阶梯现象.The interaction of copper 1,10-phenanthroline complex (Cu(OP)2) with histone H1 was studied by the resonant mirror biosensor(IAsys) and fluorescence spectrometry. The equilibrium constant and the number of binding sites were obtained at 25 ℃, pH 7.4. The results show that Cu(OP)2can bind histone H1, and the binding constant of Cu(OP)2 with histone H1 is on the order of 10^5 , and there is only one binding site between them. The affinity of Cu(OP)2 with histone H1 is about six folds higher than that of OP. It suggests that the DNA on the nucleosome is cleaved by Cu(OP)2 at the binding site with histone H1 which contribute to the DNA laddering in apoptosis induced by Cu(OP)2.
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