模拟生理条件下,利用多种光谱技术和酶活性测定法研究了新洁尔灭与过氧化氢酶的相互作用过程,探讨了二者的结合特性,过氧化氢酶空间结构和酶活性的变化.结果表明新洁尔灭对过氧化氢酶无荧光猝灭作用,其使过氧化氢酶骨架结构变松散,部分氨基酸残基微环境和蛋白二级结构发生改变,说明新洁尔灭对过氧化氢酶活性具有显著的抑制作用.从分子水平上证明了新洁尔灭可改变过氧化氢酶的结构和功能.
The interaction of bromogeramine with catalase was investigated using spectroscopic methods and enzyme activity determination under physiological conditions.We explored the characterization of the bind interaction of bromogeramine with catalase,the changes of the catalase conformation and enzyme activity.The results showed that the fluorescence of catalase can not be quenched by bromogeramine.Bromogeramine resulted in some changes of skeleton structure,secondary structure and microenvironmental of catalase,which has significant inhibitory effect on catalase activity.This study conforms that the structure and function of catalase can be changed by bromogeramine on molecular level.