摘要
用荧光光谱研究了2,4-二硝基苯肼(DNPH)与牛血清白蛋白(BSA)的相互作用。实验结果表明,2,4-二硝基苯肼能导致BSA的内源荧光猝灭,猝灭机制为静态猝灭;根据热力学参数ΔH<0、ΔS<0,得出2,4-二硝基苯肼与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2,4-二硝基苯肼使BSA分子构象发生了改变,其分子内的色氨酸和酪氨酸残基疏水作用增强。
The interaction between bovine serum albumin （ BSA ） and 2, 4-dinitrophenylhydrazine （DNPH） was investigated through fluorescence spectroscopy. The experimental results showed that the fluorescence intensity of BSA was quenched when DNPH was added. The quenching mechanism was a static quenching process. Negative enthalpy （△H） and negative entropy （△S） values indicated that both hydrogen bond and Van der Waals force played a major role in the binding of DNPH and BSA. The results of synchronous fluorescence show that the conformation of BSA has changed in the lpresenee of DNPH and the hydrophobicity around tryptophanyl and tyrosyl residues increased.
出处
《光谱实验室》
CAS
2013年第2期943-946,共4页
Chinese Journal of Spectroscopy Laboratory
基金
山东省教育厅科技计划资助项目(No.J08LG15)?
烟台市科技发展计划资助项目(2008162)
