用 U V- vis光谱和表面增强拉曼光谱研究了稀土离子和牛血清白蛋白 (BSA)的作用。紫外光谱研究表明 ,Ce4 + 、Er3+ 离子能配位诱导 BSA,使其分子中色氨酸和酪氨酸芳杂环疏水基团外露 ,2 80 nm处的吸收强度增大。当固定 BSA∶ Ce4 + 摩尔比为 1∶ 2时 ,随 BSA浓度增大 ,Ce4 + 离子配位诱导使 BSA构象发生变化 ,α-螺旋含量减少 ,致使 2 30 nm吸收峰红移 ,2 80 nm吸收峰强度增大幅度比 2 30 nm处大。拉曼光谱研究表明 ,Ce4 + 离子很可能和肽键上的 C=O基及边链羧基上的 C=O基都发生配位作用 ,并引起 BSA肽链伸展。 The effects of rare earth ions and bovine serum albumin (BSA) were investigated by UV-vis spectroscopy and surface-enhanced Raman spectroscopy. UV spectroscopy showed that Ce4 + and Er3 + ions could coordinate to induce BSA to expose the hydrophobic groups of tryptophan and tyrosine aromatic heterocycle in its molecule, and the absorption intensity at 280 nm increased. When BSA: Ce4 + molar ratio was fixed at 1: 2, the BSA conformation changed with the increase of BSA concentration, and the α-helix content decreased, resulting in a red shift at 2 30 nm and a shift of 280 nm The absorption peak intensity increased more than 2 30 nm. Raman spectroscopy studies show that Ce4 + ions are likely to coordinate with the C = O group on the peptide bond and the C = O group on the carboxyl group of the side chain, leading to the extension of the BSA peptide chain.