【摘要】 在模拟人体生理条件下,用荧光光谱法和紫外-可见吸收光谱法研究氯诺昔康(LNXC)和牛血清白蛋白(BSA)结合反应的特征。研究表明:氯诺昔康与牛血清白蛋白形成复合物,从而猝灭牛血清白蛋白的内源性荧光,该过程为静态猝灭过程。根据Stern-Volmer方程求出不同温度下结合位点数和结合常数;根据Forster非辐射能量转移理论可求出不同温度下的作用距离;通过计算相应的热力学参数,确定了氯诺昔康与牛血清白蛋白之间的作用力主要为静电引力;并利用同步荧光光谱及三维荧光光谱法探讨了氯诺昔康与牛血清白蛋白作用前后白蛋白的构象变化;此外探讨了共存金属离子对氯诺昔康与牛血清白蛋白结合作用的影响。更多还原

【Abstract】 The interaction between lornoxicam and bovine serum albumin was studied at pH 7.0 by spectroscopic methods including fluorescence spectra and UV-visible absorption spectra.It showed that the complex formation between bovine serum albumin and lornoxicam resulted in the quenching of the intrinsic fluorescence of bovine serum albumin;The main mechanism of protein fluorescence quenching was a static quenching procedure.The binding site number n and apparent binding constant KA were measured at different temperatures based on Stern-volmer equation.The distance between BSA and lornoxicam was measured at different temperatures based on the Forster nonradiative energy transfer theory.On the basis of the thermodynamic parameters,the main sorts of binding force between lornoxicam and bovine serum albumin could be judged as electrostatic force,synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structure change of bovine serum albumin with the addition of lornoxicam.In addition,the effect of some ions on the binding constant of lornoxicam with BSA was also studied.更多还原