【摘要】 用荧光光谱法、分光光度法研究了水溶液中秋水仙碱与牛血清白蛋白 (BSA)的相互结合反应。研究表明 :二者以摩尔比 1∶1牢固结合 ,其平衡常数K0 =1.92× 10 5L/mol。根据F rster非辐射能量转移机理 ,求算了给体 (BSA)与受体 (秋水仙碱 )间距离r =3.6 3nm和能量转移效率E =0 .17。实验表明 :秋水仙碱与牛血清白蛋白的相互结合作用为单一的荧光静态猝灭过程更多还原

【Abstract】 The binding reaction between colchicine and bovine serum albumins (BSA) in aqueous solution was studied by fluorescence and ultraviolet-visibale absorption spectra. The results indicates that colchicine strongly binds to BSA with a molar ratio of 1∶1 and the equilibrium constant K 0 is 1.92×10 5 L/mol. The Stern-Volmer curve on the fluorescence of BSA quenched by series of colchicine concentrations shows good linear relationship, which illustrates the combination reaction of colchicine and BSA is a single static quenching process. The shortest binding distance ( r =3.63 nm) and energy transfer efficiency ( E =0.17) between donor (BSA) and acceptor (colchicine) were obtained by Frster’s nonradiative energy transfer mechanism.更多还原