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高等学校化学研究 ›› 2002, Vol. 18 ›› Issue (1): 20-24.

• Articles • 上一篇    下一篇

Expression of a Hybrid Human Superoxide Dismutase with a High Affinity for Heparin

GOU Xiao-jun1, YIN Shao-man1, KONG Xiang-duo1, ZHU Shi-zhen1, WANG Xiao-ping1, ZHANG Hong-ying1, ZHANG Jin1, ZHU Hong2, ZHAO Chun3   

  1. 1. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130023, P. R. China;
    2. The Jilin Province People's Hospital, Changchun 130031, P. R. China;
    3. College of Chemistry, Jilin University, Changchun 130023, P. R. China
  • 收稿日期:2001-07-04 出版日期:2002-01-24 发布日期:2011-08-04

Expression of a Hybrid Human Superoxide Dismutase with a High Affinity for Heparin

GOU Xiao-jun1, YIN Shao-man1, KONG Xiang-duo1, ZHU Shi-zhen1, WANG Xiao-ping1, ZHANG Hong-ying1, ZHANG Jin1, ZHU Hong2, ZHAO Chun3   

  1. 1. Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, Jilin University, Changchun 130023, P. R. China;
    2. The Jilin Province People's Hospital, Changchun 130031, P. R. China;
    3. College of Chemistry, Jilin University, Changchun 130023, P. R. China
  • Received:2001-07-04 Online:2002-01-24 Published:2011-08-04

PDF (PC)

摘要： A designed heparin-affinity of human Cu, Zn-SOD is described. The natural leader peptide of P.leiognathi Cu, Zn-SOD and a heparin-binding peptide containing a stretch of 7 Arg were fused to the N-terminal and the C-terminal of human Cu, Zn-SOD respectively. The resulted hybrid enzyme had not only a normal SOD activity but also a high affinity for heparin eluted on the heparin-Sepharose column at 0.4 mol/L NaCl. Some properties, such as the optimum pH, the thermostability and the half-life in the circulation of rats, were also analyzed.

关键词: Human superoxide dismutase, Heparin affinity, Gene expression

Abstract: A designed heparin-affinity of human Cu, Zn-SOD is described. The natural leader peptide of P.leiognathi Cu, Zn-SOD and a heparin-binding peptide containing a stretch of 7 Arg were fused to the N-terminal and the C-terminal of human Cu, Zn-SOD respectively. The resulted hybrid enzyme had not only a normal SOD activity but also a high affinity for heparin eluted on the heparin-Sepharose column at 0.4 mol/L NaCl. Some properties, such as the optimum pH, the thermostability and the half-life in the circulation of rats, were also analyzed.

Key words: Human superoxide dismutase, Heparin affinity, Gene expression