摘要
模拟牛乳的生理环境pH6.6、37℃水浴的条件下,运用荧光光谱、同步荧光光谱和圆二色光谱法研究了青霉素与牛血清白蛋白(Bovine Serum Albumin,BSA)的相互作用。青霉素对BSA的猝灭机制属于静态猝灭,并发生分子间非辐射能量转移。热力学数据显示,二者之间的作用力主要为氢键作用;同步荧光光谱表明,青霉素与蛋白质中接近色氨酸残基的区域发生了相互作用;圆二色光谱法研究蛋白二级结构结果显示,青霉素与蛋白质结合会改变蛋白质的构象,进一步说明了青霉素在牛乳会与蛋白质作用形成稳定复合物。
The interaction between penicillin G and bovine serum albumin was studied using fluorescence spectroscopy, synchronous fluorescence spectra, and circular diehroism spectra and incubated in pH6.6, 37℃ water bath. Static quenching was predominant between penicillin G and BSA, and non-radiation energy transfer between molecules was observed. The results showed that hydrogen bond played an important role in the binding reaction. It was found that fluorescence of tryptophan residue was quenched in the interaction of penicillin with bovine serum albumin and α-casein by Synchronous Fluorescence. The study about penicillin binding BSA by CD spectroscopy proved that the binding of penicillin and protein would change the protein conformation. It was further explained that penicillin and protein form steady compound in the cow＇s milk.
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2013年第9期41-46,共6页
Food and Fermentation Industries
关键词
青霉素
牛血清白蛋白
园二色光谱
同步荧光光谱
荧光光谱
相互作用
penicillin, bovine serum albumin, CD spectroscopy, synchronous fluorescence spectroscopy, fluorescence spectroscopy, interaction
