Hu Yan-Jun, Liu Yi, Wang Jia-Bo, Xiao Xiao-He, Qu Song-Sheng
Department of Chemistry, College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
J Pharm Biomed Anal. 2004 Nov 19;36(4):915-9. doi: 10.1016/j.jpba.2004.08.021.
The interaction between monoammonium glycyrrhizinate (MAG) and bovine serum albumin (BSA) were studied by fluorescence and absorption spectroscopy. The quenching mechanism of fluorescence of bovine serum albumin by monoammonium glycyrrhizinate was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters DeltaH degrees , DeltaG degrees , DeltaS degrees at different temperatures were calculated. The distance r between donor (bovine serum albumin) and acceptor (monoammonium glycyrrhizinate) was obtained according to Forster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed.
采用荧光光谱和吸收光谱法研究了甘草酸单铵盐（MAG）与牛血清白蛋白（BSA）之间的相互作用。探讨了甘草酸单铵盐对牛血清白蛋白荧光的猝灭机制。用荧光猝灭法测定了结合位点数n和表观结合常数K。计算了不同温度下的热力学参数ΔH°、ΔG°、ΔS°。根据Förster非辐射能量转移理论得到了供体（牛血清白蛋白）与受体（甘草酸单铵盐）之间的距离r。同步荧光光谱和紫外可见吸收光谱结果表明牛血清白蛋白的构象发生了变化。
