| 紫外照射下Pb(Ⅱ)与牛血清白蛋白的相互作用研究 |
| Interaction of Pb(Ⅱ) with Bovine Serum Albumin under UV Irradiation |
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| 摘要: 通过紫外吸收光谱法、紫外二阶导数光谱法和荧光光谱法研究了生理pH值条件、紫外照射(UV C 253.7 nm)下Pb(Ⅱ)与牛血清白蛋白(BSA)的相互作用。紫外光谱和紫外二阶导数光谱显示紫外光照射改变了蛋白质中氨基酸残基的微环境。Stern-Volmer方程和Lineweaver-Burk方程分析表明，经紫外光照射后，Pb(Ⅱ)对BSA的荧光猝灭作用依然为静态猝灭作用，且没有改变其强结合位点的位置。受紫外照射过的BSA加入Pb(Ⅱ)后，BSA与Pb(Ⅱ)的结合常数(KS)随着照射时间的延长而逐渐降低；而BSA与Pb(Ⅱ)先混合后照射时，结合常数(KS)随着照射时间的延长却逐渐升高。 |
| 关键词: Pb(Ⅱ) 牛血清白蛋白 荧光猝灭 紫外-可见吸收光谱 紫外照射 |
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| Abstract: The interaction between Pb(Ⅱ) and bovine serum albumin (BSA) under the effect of UV C (253.7 nm) irradiation at physiological condition have been investigated by UV spectrum, ultraviolet second-derivative spectroscopy and fluorescence spectrum. The research results indicated that UV C irradiation make the environments of aromatic residues change according to UV spectrum and ultraviolet second-derivative spectroscopy. Stern-Volmer equation and Lineweaver-Burk equation showed that the fluorescence quenching of BSA by Pb(Ⅱ) is also a static quenching procedure and strong binding site is not change after UV C irradiation. When adding Pb(Ⅱ) to irradiated BSA, the binding constant (KS) decreased gradually; while irradiating the mixture of Pb(Ⅱ)-BSA, the binding constant (KS) increased. |
| Keywords: Pb(Ⅱ) BSA fluorescence quenching UV-Vis spectra UV C irradiation |
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| 张海蓉,边贺东,倪寿海,于 青,梁 宏,陈振峰.紫外照射下Pb(Ⅱ)与牛血清白蛋白的相互作用研究[J].无机化学学报,2009,25(2):306-311. |
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