用光谱法研究异鼠李素与牛血清白蛋白的相互作用及几种金属离子对反应的影响  

Studies on Interaction between Isorhamnetin and Bovine Serum Albumin and Effects of Several Metal Ions on Interaction by Spectrometry

作　　者：周秀清[1] 程建华[2] 孙磊[3] 徐昊妍[3] 金海燕[3] 

机构地区：[1]吉林大学测试科学实验中心,长春130021 [2]吉林大学环境与资源学院,长春130061 [3]吉林大学化学学院,长春130012

出　　处：《吉林大学学报（理学版）》2008年第5期983-987,共5页Journal of Jilin University:Science Edition

基　　金：吉林省科技发展计划项目基金(批准号:20050560)

摘　　要：用紫外光谱法、荧光光谱法研究异鼠李素与牛血清白蛋白的相互作用机理及几种金属离子与异鼠李素和牛血清白蛋白之间的相互作用,并探讨了几种金属离子与异鼠李素结合的类型,阐明了它们的结合产物对牛血清白蛋白的作用机理.实验结果表明,异鼠李素与牛血清白蛋白主要是凭借静电引力作用结合,异鼠李素主要以静态猝灭方式使牛血清白蛋白荧光强度减弱.金属离子的介入影响了异鼠李素与牛血清白蛋白的结合,降低了其结合能力.The interaction mechanisms of lsorhamnetin （ISO） and bovine serum albumin （BSA） , ISO and several metal ions as well as BSA and several metal ions were studied by means of ultraviolet-visible absorption spectrometry and fluorescence spectroscopy. These experimental results show that the static gravitation was the major force of the combination about the interaction of ISO and bovine BSA. Flourescence of BSA was quenched by ISO with the static mechanism. The binding styles of several metal ions and ISO were studied, too. It shows the binding mechanisms of some complexes of the metal ions and ISO with BSA. It indicates that the inlerventions of metal ions affected the combination of ISO and BSA, they depressed their abilities of combination.

关 键 词：异鼠李素 牛血清白蛋白 荧光猝灭 结合常数 结合位点数 

分 类 号：O657.3[理学—分析化学]