Study on Binding Reaction between Flucytosine and Bovine Serum Albumin  

作　　者：颜承农 张华新 梅平 刘义 

机构地区：[1]College of Chemistry and Environmental Engineering, Yangtze University, Jingzhou, Hubei 434020, China [2]College of Chemistry and Molecular Sciences, Wuhan University, Wuhan, Hubei 430072, China

出　　处：《Chinese Journal of Chemistry》2005年第9期1151-1156,共6页中国化学（英文版）

基　　金：Project supported by the National Natural Science Foundation of China （No. 20373051） and the National Natural Science Foundation of Hubei Province in China （No. 2005ABA067）.

摘　　要：The binding of flucytosine to bovine serum albumin （BSA） was studied by means of fluorescence and absorption spectra under the conditions of simulant clay physiology. It showed a powerful ability to quench the fluorescence launching from BSA. After analyzing the fluorescence quenching data by Stem-Volmer equation and Lineweaver-Burk double-reciprocal equation, it was found that they matched the latter better and so they belonged to static quenching. The binding constant was calculated to be 5.710 × 10^3 L·mol^-1 at 297 K. The binding locality was a distance 2.49 nm away from tryptophan residue-212 based on Foster＇s non-radiation energy transfer mechanism. The binding power is mainly the hydrogen bond and van der Waals force according to the thermodynamic parameters. The information of BSA conformation was acquired by synchronous fluorescence spectrum and three-dimensional fluorescence spectrum.The binding of flucytosine to bovine serum albumin （BSA） was studied by means of fluorescence and absorption spectra under the conditions of simulant clay physiology. It showed a powerful ability to quench the fluorescence launching from BSA. After analyzing the fluorescence quenching data by Stem-Volmer equation and Lineweaver-Burk double-reciprocal equation, it was found that they matched the latter better and so they belonged to static quenching. The binding constant was calculated to be 5.710 × 10^3 L·mol^-1 at 297 K. The binding locality was a distance 2.49 nm away from tryptophan residue-212 based on Foster＇s non-radiation energy transfer mechanism. The binding power is mainly the hydrogen bond and van der Waals force according to the thermodynamic parameters. The information of BSA conformation was acquired by synchronous fluorescence spectrum and three-dimensional fluorescence spectrum.

关 键 词：FLUCYTOSINE bovine serum albumin fluorescence spectroscopy three-dimensional fluorescence spectrum thermodynamic parameter 

分 类 号：O629.73[理学—有机化学] O657.34[理学—化学]