茜素黄与牛血清白蛋白相互作用特征的荧光光谱法研究

Study on Action Features between Alizarin Yellow Rlnd and Bovine Serum Albumin Each Other by Fluorescence Spectrophtometry

用荧光光谱、同步荧光光谱、三维荧光光谱和紫外可见吸收光谱法等研究了茜素黄（AlizarinYellow R,AYR）与牛血清白蛋白（bovine serumalbumin,BSA）相互作用,扫描AYR和AYR作用于BSA的荧光猝灭光谱、同步荧光光谱、三维荧光光谱和紫外-可见吸收光谱,证实了AYR有很强地猝灭BSA荧光强度的能力,分别用Stern-Vol mer方程、Lineweaver-Burk双倒数方程和热力学方程等处理试验数据,证实了在实验条件下,AYR与BSA可相互作用形成具有一定结构的复合物,作用力主要是静电作用力,得到在21~41℃温度范围内相互作用的荧光猝灭结合常数KLB（平均值为4.394×104mol/L）,相互作用的热力学函数变化ΔHθ、ΔGθ和ΔSθ的平均值分别为-3.408kJ/mol、-27.02kJ/mol和77.64J/K,结合位点数（平均值）为1.183。这为研究AYR的染色机理、探讨释放到环境中的AYR所产生的生物学效应以及对生物体蛋白质构象的影响等提供重要信息。

The action of Alizarin Yellow Rlnd(AYR)to bovine serum albumin(BSA)was studied by the fluorescence spectroscopy,three-dimensional fluorescence spectrum,synchronous fluorescence spectrum and ultra-violet spectrum.It was shown that this compound had a quite strong ability to quench the fluorescence launching from BSA.After analyzing and processing the fluorescence quenching data according to Sterm-Volmer equation,Lineweaver-Burk equation and thermodynamic equation,the binding constant and thermodynamic parameters from 21℃ to 41℃ were obtained.the average value of binding constant(KLB:4.394×104KJ·mol-1),thermodynamic parameters(ΔH θ:-3.408 KJ·mol-1,ΔG θ:-27.02KJ·mol-1 and ΔSθ:77.64J·K-1)and amounts of binding sites(1.183)were obtained in this paper.It provides important information for the configuration modification of BSA because added AYR,biology effects in a living body and coloration mechanism of AYR.