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用荧光光谱法、紫外光谱法研究了生理条件下维生素C(Vc)与牛血清白蛋白(BSA)相互作用的光谱特性。测定了Vc与BSA在21、34℃两个温度下的结合常数KA(21℃:4.381×105L/mol,34℃:4.061×105L/mol)和结合位点数n(21℃:1.08,34℃:1.10)。结果表明:Vc对BSA有明显的猝灭作用,其方式为静态猝灭。通过热力学分析得出Vc与BSA之间主要作用力是静电引力。同步荧光分析发现Vc的存在改变了牛血清白蛋白的分子构象。
The spectral characteristics of the interaction between vitamin C (Vc) and bovine serum albumin (BSA) under physiological conditions were studied by fluorescence spectroscopy and ultraviolet spectroscopy. The binding constants KA (21 ℃: 4.381 × 105L / mol, 34 ℃: 4.061 × 105L / mol) and the number of binding sites n (21 ℃: 1.08, 34 ℃) between Vc and BSA at 21 and 34 ℃ were measured. : 1.10). The results show that Vc has obvious quenching effect on BSA by static quenching. Thermodynamic analysis shows that the main force between Vc and BSA is electrostatic attraction. Synchronous fluorescence analysis revealed that the presence of Vc changed the molecular conformation of bovine serum albumin.