Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering, Shandong University, China-America CRC for Environment & Health, Shandong Province, Jinan 250100, People's Republic of China.
J Biochem Mol Toxicol. 2011 Jul-Aug;25(4):263-8. doi: 10.1002/jbt.20385. Epub 2011 Feb 9.
The interaction of Ce(3+) to bovine serum albumin (BSA) has been investigated mainly by fluorescence spectra, UV-vis absorption spectra, and circular dichroism (CD) under simulative physiological conditions. Fluorescence data revealed that the quenching mechanism of BSA by Ce(3+) was a static quenching process, the binding constant is 6.70 × 10(5) , and the number of binding site is 1. The thermodynamic parameters (ΔH = -29.94 kJ mol(-1) , ΔG = -32.38 kJ mol(-1) , and ΔS = 8.05 J mol(-1) K(-1) ) indicate that electrostatic effect between the protein and the Ce(3+) is the main binding force. In addition, UV-vis, CD, and synchronous fluorescence results showed that the addition of Ce(3+) changed the conformation of BSA.
在模拟生理条件下，主要通过荧光光谱、紫外-可见吸收光谱和圆二色性（CD）研究了 Ce(3+) 与牛血清白蛋白（BSA）的相互作用。荧光数据表明，Ce(3+) 猝灭 BSA 的机制是静态猝灭过程，结合常数为 6.70×10(5)，结合位点数为 1。热力学参数（ΔH = -29.94 kJ mol(-1)，ΔG = -32.38 kJ mol(-1)，ΔS = 8.05 J mol(-1) K(-1)）表明，蛋白质与 Ce(3+) 之间的静电作用是主要的结合力。此外，紫外-可见、CD 和同步荧光结果表明，Ce(3+) 的加入改变了 BSA 的构象。
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