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 2,4-dinitrophenylhydrazine (DNPH) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy. The experimental results showed that 2,4-dinitrophenylhydrazine quenched the endogenous fluorescence of BSA and the quenching mechanism was quiescent quenching. According to the thermodynamic parameters ΔH <0 and ΔS <0, 2,4-dinitro The main interaction between phenylhydrazine and BSA was hydrogen bond and van der Waals forces. The results of synchronous fluorescence showed that 2,4-dinitrophenylhydrazine changed the conformation of BSA, and the intramolecular tryptophan and tyramine Acid residue enhances the hydrophobic effect.