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投稿时间：2015-04-10
投稿时间：2015-04-10
中文摘要: 采用荧光光谱法考察Fe3+对VB1与牛血清白蛋白（BSA）相互作用的影响。试验结果表明，VB1对BSA的内源性荧光有猝灭作用，猝灭类型为动态猝灭，作用力类型为氢键和范德华力。Fe3+的加入并未改变VB1对BSA的猝灭类型和作用力类型，但对其猝灭速率常数（kq）、结合常数（KA）以及结合位点数（n）会有不同程度的影响。同步荧光光谱显示VB1主要与BSA中的色氨酸残基作用，引起其构象或周围环境的改变。
Abstract:The interactionofVB1and bovine serum albumin（BSA）was studied in the presence of Fe3+by fluorescence spectroscopy.The results indicated that VB1could quench the intrinsic fluorescence of BSA，the quenching mechanism was static quenching and the main binding force was hydrogen bond and Vander Waals.The fluorescence quenching mechanism and the main binding force were not changed in the presence of Fe3+，but the quenching rate constant（k）q，the binding constants（KA）and the binding sites（n）were changed in different degrees.Synchronous spectra showedthatVB1binded to tryptophan residue and changed its microenvironment.
keywords: VB1 bovine serum albumin Fe3+ fluorescence spectroscopy
文章编号：201610012 中图分类号： 文献标志码：
基金项目:安阳工学院青年科研基金项目（201318）
| Author Name | Affiliation |
| GUO Yu-hua，YU You-zhu，NIU Yong-sheng | College of Chemistry and Environmental Engineering，Anyang Institute of Technology，Anyang 455000，Henan，China |
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