5 L/mol、1.12,其作用力以疏水作用為主。同步熒光光譜法測定的結(jié)合位點(diǎn)靠近色氨酸,并使色氨酸的疏水性增強(qiáng)。結(jié)論 牡荊苷與溶菌酶結(jié)合并改變?nèi)芫傅臉?gòu)象,共存金屬離子對牡荊苷與溶菌酶的相互作用有一定的影響。;Objective To study the spectroscopic characteristics of interaction between vitexin and lysozyme under the simulative human physiological condition. Methods Interaction mechanism and interaction force of vitexin with lysozyme were investigated by fluorescence spectroscopy and synchronous fluorescence spectroscopy. The effects of their interaction on conformation change of lysozyme were investigated. Results The fluorescence quenching mechanism of vitexin with lysozyme was static quenching. The binding parameters of vitexin and lysozyme were as following:The binding constant (K) was 6.73×105 L/mol, and the number of binding site was 1.12, respectively. And the major driving force was hydrophobic force. The Results of synchronous fluorescence demonstrated that the binding site was closer to tryptophan residues and the hydrophobicity of tryptophan residues was increased. Conclusion Vitexin with lysozyme can form complex and change the conformation of lysozyme. The common metal ions have effects on interaction between vitexin and lysozyme."/>