论文部分内容阅读
用荧光光谱法和紫外吸收光谱法研究了在生理pH值条件下氨与牛血清白蛋白(BSA)的相互作用。结果表明:氨对BSA的荧光有较强的猝灭作用,该猝灭属于同时具有动态猝灭和静态猝灭特征的联合猝灭,但以静态猝灭为主。根据猝灭结果求得了不同温度下氨与BSA相互作用的结合位点数、结合常数及反应热力学参数,并据此推测它们之间主要的相互作用力为范德华力和氢键。计算出当氨与BSA处于等摩尔浓度时两种分子间的作用距离为6.3126nm,它们之间发生了非辐射能量转移。同步荧光光谱图显示,氨对BSA的构象有影响。
The interaction between ammonia and bovine serum albumin (BSA) at physiological pH was studied by fluorescence spectroscopy and ultraviolet absorption spectroscopy. The results show that ammonia quenches the fluorescence of BSA strongly. The quenching belongs to the combined quenching with both dynamic and static quenching, but mainly static quenching. According to the quenching results, the binding sites, binding constants and reaction thermodynamic parameters of the interaction between ammonia and BSA at different temperatures were obtained, and the main interaction forces between them were assumed to be van der Waals forces and hydrogen bonds. It is calculated that when the ammonia and BSA are in equimolar concentrations, the interaction distance between the two molecules is 6.3126 nm, and non-radiative energy transfer occurs between them. Synchronous fluorescence spectra show that ammonia has an influence on the conformation of BSA.