Acta Chimica Sinica ›› 2005, Vol. 63 ›› Issue (1): 1-4.     Next Articles



亓昭鹏1,周青2,杜江燕3,陆天虹ac,李邨1,陈蕴2,黄晓华*1 2   

  1. (1南京师范大学化学与环境科学学院 南京 210097)
    (2江南大学工业生物技术教育部重点实验室 无锡 214036)
    (3中国科学院长春应用化学研究所 长春 130022)
  • 投稿日期:2004-04-13 修回日期:2004-10-25 发布日期:2010-12-10
  • 通讯作者: 黄晓华

Study on Interaction Ways between Tb3+and Horseradish Peroxidase

QI Zhao-Peng1, ZHOU Qing2, DU Jiang-Yan3, LU Tian-Hong1,3, LI Cun1, CHEN Yun2, HUANG Xiao-Hua*1,2   

  1. (1 Department of Chemistry, Nanjing Normal University, Nanjing 210097)
    (2 Key Laboratory of Industrial Biotechnology, Ministry of Education, Southern Yangtze University, Wuxi 214036)
    (3 Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022)
  • Received:2004-04-13 Revised:2004-10-25 Published:2010-12-10
  • Contact: HUANG Xiao-Hua

The interaction ways between Tb3+and horse radish peroxidase (HRP) were investigated for the first time using UV-Vis absorption spectroscopy, fluorescence spectroscopy, atomic absorption spectroscopy and enzyme separation technique. The experimental results indicated that there are three interaction ways between Tb3+and HRP. Firstly, Tb3+would bind to N or O atoms in the polypeptide of HRP. It would affect the conformation of HRP. Secondly, Tb3+can replace Ca2+partially. Thirdly, Tb3+would shear the polypeptide and thus change the structure of HRP. Therefore, Tb3+may interact with HRP in one way mainly or three ways simultaneously.

Key words: Tb3+, horseradish peroxidase, enzyme activity, interaction way