【摘要】 用荧光光谱法研究了三羟基苯基荧光酮(TH-PF)-钼(Ⅵ)配合物与牛血清白蛋白的结合反应。探讨了TH-PF-Mo(Ⅵ)配合物对蛋白质内源荧光的猝灭机理,并测定了不同温度下的结合常数,温度为25℃时,荧光猝灭法测得该反应的结合常数为K=4.78×104L.mol-1,温度为40℃时,荧光猝灭法测得该反应的结合常数为K=3.72×104L.mol-1。根据F rster非辐射能量转移理论,确定了给体-受体之间的作用距离和能量转移效率(E=0.314),并根据热力学参数确定了TH-PF-Mo(Ⅵ)配合物与牛血清白蛋白之间的作用力类型,以静电引力为主。更多还原

【Abstract】 The mechanism of interaction between bovine serum albumin（BSA） and trihydroxylphenylfluorone（TH-PF）-Mo（Ⅵ） complex in neutral solution was studied by fluorimetric method.The mechanism of fluorescence quenching of BSA caused by（TH-PF）-Mo（Ⅵ） complex probe was investigated and the binding constants under different temperature were measured.The binding constants of the reaction at 25 ℃ and 40 ℃ were calculated by fluorimetric method to be 4.78×10⁴ L·mol^-1 and 3.72×10⁴ L·mol^-1,respectively.According to the theory of Frster non-radiation energy transfer,the binding distance and transfer efficiency at 25 ℃ were calculated to be 2.89 nm and 0.314,respectively.Furthermore,the thermodynamic parameters were measured and the results indicated that electrostatic force played a major role in the interaction between TH-PF-Mo（Ⅵ） complex and BSA.更多还原