盐酸苯肼与牛血清白蛋白相互作用的研究  

The interactions between phenylhydrazine hydrochloride and bovine serum albumin

作　　者：付彩霞[1] 王晓艳[1] 高宗华[1] 

机构地区：[1]滨州医学院化学教研室,山东烟台264003

出　　处：《化学研究与应用》2013年第5期642-646,共5页Chemical Research and Application

基　　金：山东省教育厅科技计划项目(J08LG15)资助;烟台市科技发展计划项目(2008162)资助

摘　　要：用荧光光谱及紫外光谱研究了盐酸苯肼与牛血清白蛋白(BSA)的相互作用。实验结果表明,盐酸苯肼能导致BSA的内源荧光猝灭,猝灭机制为静态猝灭;根据热力学参数△H<0、△S<0,得出盐酸苯肼与BSA之间的主要作用力为氢键和范德华力。同步荧光的结果表明盐酸苯肼使BSA分子构象发生了改变,色氨酸和酪氨酸残基所处环境的疏水性降低。紫外光谱法进一步证明了其猝灭机制为静态猝灭。The interactions between phenylhydrazine hydrochloride and bovine serum albumin （BSA）were investigated using fluores- cence spectroscopy and ultraviolet spectroscopy. The experimental results showed that the fluorescence intensity of BSA was quenched when phenylhydrazine hydroehloride was added. The quenching mechanism was a static quenching process. Negative en- thalpy （AH） and negative entropy （AS） values indicated that both hydrogen bond and Van der Waals force played a major role in the binding of phenylhydrazine hydrochloride and BSA. The results of synchronous fluorescence showed that the conformation of BSA has changed in the presence of phenylhydrazine hydroehloride and the hydrophobicity around tryptophanyl and tyrosyl residues reduced. The results of absorption spectra also confirmed that the quenching mechanism was static quenching process.

关 键 词：盐酸苯肼 牛血清白蛋白 相互作用 

分 类 号：O657.3[理学—分析化学]