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目的:通过对锌(Ⅱ)、水杨酸和牛血清白蛋白的结合反应的研究,进一步探讨了水杨酸、锌(Ⅱ)在生物体内与蛋白质相互作用的机理。方法:在模拟生理条件下,用荧光光谱法研究了水杨酸对牛血清白蛋白以及锌(Ⅱ)对水杨酸和牛血清白蛋白荧光光谱特性的影响。结果:实验结果表明,水杨酸和锌(Ⅱ)都可以使牛血清白蛋白的荧光强度发生猝灭。根据荧光猝灭双倒数图计算水杨酸和牛血清白蛋白之间的结合常数为4.682×104,结合位点数为1.12。结论:由此可见,水杨酸和牛血清白蛋白之间有很强的结合作用,这为水杨酸在体内被蛋白质储存和转运提供了条件。在锌(Ⅱ)存在下,水杨酸与牛血清白蛋白的结合作用有所减弱。荧光猝灭双倒数图计算的结果表明,水杨酸和牛血清白蛋白之间的结合常数随锌(Ⅱ)浓度的增大而减小。
OBJECTIVE: To further explore the mechanism of the interaction between salicylic acid and zinc (Ⅱ) and proteins in vivo through the study of the binding reaction of zinc (Ⅱ), salicylic acid and bovine serum albumin. Methods: Fluorescence spectroscopy was used to study the effect of salicylic acid on the fluorescence spectra of salicylic acid and bovine serum albumin (BSA) and zinc (Ⅱ) under simulated physiological conditions. Results: The experimental results show that both salicylic acid and zinc (Ⅱ) can quench the fluorescence intensity of bovine serum albumin. The binding constant between salicylic acid and bovine serum albumin was 4.682 × 104 and the number of binding sites was 1.12 according to double-reciprocal fluorescence quenching. Conclusion: This shows that there is a strong binding between salicylic acid and bovine serum albumin, which provided the conditions for salicylic acid to be stored and transported by the protein in vivo. In the presence of zinc (II), the binding of salicylic acid to bovine serum albumin is weakened. Fluorescence quenching dual reciprocal graph calculated results show that the binding constant between salicylic acid and bovine serum albumin with zinc (Ⅱ) concentration decreases.