Abstract：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.
卢秀敏,陈得军,王公轲,杨海艳,卢雁*. 诺氟沙星与卵清蛋白相互作用的研究[J]. 光谱学与光谱分析, 2009, 29(01): 236-239.
LU Xiu-min,CHEN De-jun,WANG Gong-ke,YANG Hai-yan,LU Yan*. Studies on the Reaction of Norfloxacin with Ovalbumin. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2009, 29(01): 236-239.
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