摘要
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： According to Stern - Volmer equation and double - reciprocal equation, the concentration of Znic （Ⅱ ） is denser, and the binding constant （K） are smaller. By studying the binding interaction between Zinc （ Ⅱ）, BHA and BSA, the mechanism of the interaction among BHA, Zinc （Ⅱ ） and protein in organism, is furtherly discussed. Methods： The interaction between salicylic acid and bovine serum albumin, and the influence of Zinc （ Ⅱ ） on the system of salicylic acid and bovine serum albumin was studied under physiological condition by fluorescence method. Results：It was shown that salicylic acid has a powerful ability to quench the BSA fluorescence via a nonradiative energy transfer mechanism. The fluorescence quenching data were analyzed according to Stern -Volmer equation and double -reciprocal equation, and the binding constant （K） and the binding sites （n） were obtained. In the system of binary complex of BHA and BSA, K =4. 682 × 10^4, and n = 1.12. Conclusion：There is a strong combination between BHA and BSA, which offers the condition for the serum protein to be deposited and transported in vivo. Meanwhile, the combination between BHA and BSA becomes weaker in the presence of Zinc （ Ⅱ ）.
出处
《中国卫生检验杂志》
CAS
2009年第9期1967-1968,共2页
Chinese Journal of Health Laboratory Technology
