摘要
利用荧光光谱和紫外-可见光谱法研究了巯嘌呤药物与牛血清白蛋白(BSA)和人血清白蛋白(HSA)分子间的相互结合反应。测得巯嘌呤与BSA、HSA反应的结合平衡常数分别为:2.39×103L/mol、1.28×103L/mol。根据F rster非辐射能量转移理论,求算了给体(BSA和HAS)与受体(巯嘌呤)间的结合距离和能量转移效率。用同步荧光法考察了巯嘌呤对BSA和HAS构象的影响。证实了巯嘌呤药物与牛血清白蛋白和人血清白蛋白的相互结合作用为单一的静态猝灭过程。
The binding characteristics between 6-Mercaptopurine and bovine serum albumins （human serum albumin） have been studied by fluorescence spectroscopy. The equilibrium constant Ka and the number of binding sites n have been measured. The binding distance between 6-Mercaptopurine and BSA （HSA） and the transfer efficiency have been obtained based on the mechanism of Forster energy transfer. The effect of 6-Mercaptopurine on the conformation of BSA and HSA has also been analyzed using synchronous fluorescence spectroscopy. The studies indicate that the combination reaction of 6-Mercaptopurine with BSA and HSA is a single static quenching process and 6-Mercaptopurine can affect the conformation of bovine serum albumin and human serum albumin.
出处
《分析科学学报》
CAS
CSCD
2008年第5期549-552,共4页
Journal of Analytical Science
基金
国家自然科学基金(No.20575037)
山西高校科技研究开发项目(200713006)
关键词
荧光猝灭
巯嘌呤
牛血清白蛋白
人血清白蛋白
Fluorecence spectroscopy
6-Mercaptopurine
Bovine serum albumin
Human serum albumin
