应用荧光光谱法和紫外光谱法研究了诺氟沙星(NRF)与卵清蛋白(OVA)的相互作用,计算了诺氟沙星与卵清蛋白之间的结合常数和结合位点数。实验发现卵清蛋白的最大发射峰位于338 nm,当向该溶液中滴加诺氟沙星时,该发射峰强度明显减弱,且向长波长方向稍有移动。实验表明:随着温度升高,卵清蛋白的猝灭曲线斜率降低,证实了诺氟沙星与卵清蛋白的相互作用为单一的静态猝灭过程,同时随着溶液pH值的增大,诺氟沙星对卵清蛋白的猝灭程度逐渐降低。根据热力学参数确定了诺氟沙星与卵清蛋白之间主要以静电作用力相结合。最后利用紫外光谱法证明了诺氟沙星对卵清蛋白构象产生了影响。

The interaction between norfloxacin (NRF) and ovalbumin (OVA) was studied by fluorescence and absorption spectroscopy.The binding constants and the binding sites were measured by fluorescence quenching method.It was found that the emission peak of OVA was positioned at 338 nm.When the norfloxacin was added into OVA solution gradually,the intensity of 338 nm emission peak of OVA decreased obviously and moved towards long wavelength.The experiment demonstrated that the higher the temperature,the lower the slopes of quenching curves of OVA in the presence of different amounts of NRF.It was confirmed that the combination of NRF with OVA is a single static quenching process.With the increase in the pH of the solution,the quenching efficiency decreased in the binding.From thermodynamic parameters,it can be judged that the binding power between OVA and NRF is electrostatic effect and H-bond formation.The UV-Vis absorption spectra of OVA in the presence of NRF show that the conformation of OVA changed.