摘要
利用荧光和紫外吸收光谱法研究了苯佐卡因与牛血清白蛋白的相互结合作用。测定了两者的结合位点数(n)和结合常数(Ka),结果分别为0.87和1.11×10~4L·mol^(-1),该结果表明复合物中苯佐卡因和牛血清白蛋白的结合比约为1∶1;不同温度下淬灭常数(kq)分别为1.52×1012L·mol^(-1)·s^(-1)(p H 7.4,291 K)和1.39×1012L·mol^(-1)·s^(-1)(p H 7.4,310 K),表明苯佐卡因与牛血清白蛋白作用过程中荧光猝灭为静态淬灭。结合同步荧光光谱分析,讨论了苯佐卡因对蛋白质构象的影响,结果表明苯佐卡因的存在对牛血清白蛋白中酪氨酸和色氨酸残基附近的微环境影响不明显。
The interaction between benzocaine （BZC） and bovine serum albumin （BSA） was investiga- ted by fluorescence and ultraviolet-visible spectroscopy. The number of binding sites n （0.87） and bind- ing constant （Ks, 1.11 × 104 L mol-1） were calculated through fluorescence quenching method, which indicates that the molar ratio of BSA to BZC in complex is about 1 ： 1. The biological macromolecule quenching constants （kq） were measured to be 1.52 × 1012 L mol-1 s-1 （pH 7.4, 291 K） and 1.39 ×1012 L mol-1 s-1 （pH 7.4, 310 K）, respectively. The results indicated that the combination reaction between BZC and BSA was a static quenching process. And, the change of the conformation of BSA was a/so studied by synchronous fluorescence spectroscopy, the results showed that the presence of BZC didn＇t affect the microenvironment around the tyrosine and tryptophan residues.
出处
《黑龙江大学自然科学学报》
CAS
北大核心
2016年第4期527-532,共6页
Journal of Natural Science of Heilongjiang University
基金
Supported by the National Natural Science Foundation of China(81460552)
the Foundation of Guizhou Science and Technology Department([2013]2320
[2014]2174)
关键词
苯佐卡因
牛血清白蛋白
荧光光谱
同步荧光光谱
benzocaine
bovine serum albumin
fluorescence spectroscopy
synchronous fluorescence spectroscopy
