【摘要】 运用荧光光谱法研究了铁(Ⅲ,Fe3+)与牛血清白蛋白(Bovine Serum Albumin,BSA)的相互作用。在290K、308K时,随着Fe3+浓度的增大BSA发射峰略有蓝移,荧光强度降低,根据Stern-Volmer方程求出了Fe3+对牛血清白蛋白(BSA)荧光猝灭的常数,并探讨了BSA荧光猝灭机制,为静态猝灭,温度没有改变Fe3+对BSA的猝灭机制。根据公式lg(F0/F-1)=lgKA+nlg[C]求出了二者在两个温度时的结合常数(KA)以及结合位点数(n),经过数据分析后,得到了三个热力学参数吉布斯自由能变(ΔG)、焓变(ΔH)和熵变(ΔS),结果表明温度升高Fe3+与BSA的作用增强,二者之间的作用力主要为疏水作用。更多还原

【Abstract】 The interaction between iron(Ⅲ,Fe3+) and bovine serum albumin(BSA) has been investigated by the fluorescence spectrum.The maximum emission wavelength of BSA was little blue-shift,and the maximum emission intensity of BSA declined with adding the concentration of Fe3+.According to Stern-Volmer equation,the quenching constant was obtained.The fluorescence of BSA was quenched by Fe3+,and the quenching mechanism of BSA was a static quenching machenism.On the basis of lg(F0/F-1)=lgKA+nlg[C] and relevant thermodynamics formula,the association constant(KA),the number binding site(n) and thermodynamic datas(ΔG,ΔH and ΔS) were obtained respectively.After the quenching datas were analyzed,it has been suggested that the conjugation of Fe3+ and BSA enhanced with elevating the tempreture and the acting force was mainly hydrophobic force.更多还原