School of Environmental Science and Engineering, Shandong University, 27 Shanda South Road, Jinan 250100, People's Republic of China.
J Biochem Mol Toxicol. 2010 Jan-Feb;24(1):66-71. doi: 10.1002/jbt.20314.
The toxic effects of ethanol on bovine serum albumin (BSA) were measured by resonance light scattering (RLS), fluorescence spectroscopy, ultraviolet spectrophotometry (UV), circular dichroism (CD), and transmission electron microscopy (TEM). The results indicated that ethanol had toxic effects on BSA, which led to protein denaturation and the effects increased with the ethanol dose. By means of RLS, BSA was found to aggregate in the presence of ethanol and particles smaller than 100 nm were observed from TEM. The fluorescence spectra showed that the intensity of the characteristic peak of BSA decreased and blue shifted, because of changes in the BSA skeleton structure, as well as alteration of the microenvironment of tryptophan (Trp) residues. The conformation changes of BSA were also shown by UV and CD spectrometry.
采用共振光散射（RLS）、荧光光谱、紫外分光光度法（UV）、圆二色性（CD）和透射电子显微镜（TEM）研究了乙醇对牛血清白蛋白（BSA）的毒性作用。结果表明，乙醇对 BSA 具有毒性作用，导致蛋白质变性，且随着乙醇剂量的增加而增强。通过 RLS 发现，在乙醇存在的情况下 BSA 会聚集，并且 TEM 观察到小于 100nm 的颗粒。荧光光谱表明，由于 BSA 骨架结构的变化以及色氨酸（Trp）残基微环境的改变，BSA 特征峰的强度降低且蓝移。紫外和 CD 光谱也表明了 BSA 构象的变化。
