化学学报 ›› 2004, Vol. 62 ›› Issue (14): 1318-1322. 上一篇    下一篇

外源镧(Ⅲ)对辣根过氧化物酶的结构的影响

夏炳乐, 彭敦耕, 郑晓云, 肖厚荣, 盛良全, 刘清亮   

  1. 中国科学技术大学化学系, 合肥, 230026
  • 投稿日期:2003-05-07 修回日期:2004-03-17 发布日期:2014-02-17
  • 通讯作者: 夏炳乐,E-mail:xiabl@ustc.edu.cn;彭敦耕,E-mail:dgpeng@ustc.edu E-mail:xiabl@ustc.edu.cn;dgpeng@ustc.edu
  • 基金资助:
    国家烟草专卖局科研基金(No.1002001041)资助项目.

Effect of Extraneous Lanthanum(Ⅲ) on the Structure of Horseradish Peroxidase

XIA Bing-Le, PENG Dun-Geng, ZHENG Xiao-Yun, XIAO Hou-Rong, SHENG Liang-Quan, LIU Qing-Liang   

  1. Department of Chemistry, University of Science and Technology of China, Hefei 230026
  • Received:2003-05-07 Revised:2004-03-17 Published:2014-02-17

运用荧光光谱、傅立叶变换红外光谱以及曲线拟合等技术研究了镧离子对辣根过氧化物酶的结构的影响.结果表明荧光增强的原因是由于镧离子的加入使镧离子和酶结合,酶的二级结构发生变化,导致荧光发色基团所处的微环境也相应变化;并运用它推测了镧离子对该酶的激活作用机制.

关键词: 辣根过氧化物酶, 镧(Ⅲ), 结合, 微环境, 二级结构

Through the fluorescence spectra, FT-IR spectra and curve-fit, the effect of lanthanum(Ⅲ) on horseradish peroxidase (HRP) was studied.It is concluded that the reason of the stimulation is due to the binding of La(Ⅲ) to HRP, which induced the changes of the enzyme's secondary structure and the microenvironment of the fluorophore, while adding La(Ⅲ) into the HRP.The activation mechanism of La(Ⅲ) to the HRP was also discussed.

Key words: horseradish peroxidase, lanthanum(Ⅲ), binding, microenvironment, secondary structure