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用同步荧光法消除了溴氰菊酯对牛血清白蛋白内源性荧光的干扰,研究了生理条件(pH=7.4)下溴氰菊酯与牛血清白蛋白之间的相互作用。不同温度下的猝灭常数证明溴氰菊酯对牛血清白蛋白的猝灭是静态过程,据此求得25℃下溴氰菊酯与牛血清白蛋白的结合常数为1.97×105L.mol-1,热力学参数ΔH=29.79kJ.mol-1、ΔS=201.32J.K-1.mol-1,两者之间的相互作用力以疏水作用力为主。根据Foerster非辐射能量转移机理,计算了牛血清白蛋白与溴氰菊酯间结合距离r=5.42nm,能量转移效率E=0.104。
Synchronous fluorescence method was used to eliminate the interference of deltamethrin on endogenous fluorescence of bovine serum albumin. The interaction between deltamethrin and bovine serum albumin under physiological conditions (pH = 7.4) was studied. The quenching constants at different temperatures showed that the quenching of bovine serum albumin by deltamethrin was a static process, and the binding constant of deltamethrin with bovine serum albumin at 25 ℃ was 1.97 × 105L.mol- 1, the thermodynamic parameters ΔH = 29.79kJ.mol-1, ΔS = 201.32JK-1.mol-1, the interaction between the two to hydrophobic force-based. According to the Foerster non-radiative energy transfer mechanism, the binding distance between bovine serum albumin and deltamethrin was calculated to be 5.42nm, and the energy transfer efficiency E = 0.104.