采用荧光光谱法研究了烟酸(NTA)与牛血清白蛋白(BSA)之间的相互作用.结果表明,NTA主要以动态猝灭的方式使BSA的内源性荧光下降.通过计算得出了在测定温度(T)为293和310 K时,NTA与BSA的结合常数(K)分别为31.9和72.9 L·mol-1.根据热力学参数确定了NTA与BSA之间以疏水力相互作用.同步荧光光谱与紫外光谱技术分析表明,NTA对BSA的构象几乎没有影响.%The interaction between nicotinic acid (NTA) and bovine serum albumin (BSA) in physiological solution was investigated by fluorescence spectrometry. The results showed fluorescence intensity of BSA was quenched by NTA based on the dynamic quenching model. The binding constants were obtained by calculation, which were 31.9 (293 K) and 72.9 L·mol-1 (310 K) respectively. The thermodynamic parameters obtained from measured data showed that the interaction of NTA and BSA was mainly driven by hydrophobic force. Synchronous fluorescence spectrometry and ultraviolet (UV) spectroscopy indicated that NTA did not affect the conformation of BSA.
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