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模拟生理条件下,应用荧光光谱法研究了芬布芬对牛血清白蛋白,铜(Ⅱ)对牛血清白蛋白以及铜(Ⅱ)对芬布芬和牛血清白蛋白荧光光谱特性的影响。实验表明:铜(Ⅱ)和芬布芬均可使牛血清白蛋白的荧光强度发生静态猝灭,并且在铜(Ⅱ)存在下,芬布芬对牛血清白蛋白的荧光猝灭作用显著增强。根据荧光猝灭双倒数图计算芬布芬和牛血清白蛋白的结合常数为8.44×104,结合位点数为0.97。荧光猝灭双倒数图计算的结果表明,芬布芬和牛血清白蛋白之间的结合常数和结合位点数均随铜(Ⅱ)浓度的增大而增大。很据三者结合反应的研究,进一步探讨了芬布芬、铜(Ⅱ)在生物体内与蛋白质相互作用的机理。
Under simulated physiological conditions, the effect of fenbufen on the fluorescence spectra of bovine serum albumin, copper (Ⅱ) to bovine serum albumin and copper (Ⅱ) to fenbufen and bovine serum albumin was studied by fluorescence spectroscopy. The results showed that both copper (Ⅱ) and fenbufen could quench the fluorescence intensity of bovine serum albumin, and the fluorescence quenching effect of fenbufen on bovine serum albumin was significantly enhanced in the presence of copper (Ⅱ) . The binding constant of fenbufen and bovine serum albumin was 8.44 × 104 and the number of binding sites was 0.97 according to double-reciprocal fluorescence quenching. Fluorescence quenching dual reciprocal graph calculated results showed that the binding constant and the number of binding sites between the fenbufen and bovine serum albumin with copper (Ⅱ) concentration increases. According to the combination of the three studies, we further explored the mechanism of the interaction between fenbufen and copper (Ⅱ) in vivo.