Chem. J. Chinese Universities

• 研究论文 • Previous Articles     Next Articles

Molecular Modification and Expression of Human CuZn Superoxide Dismutase in pichia pastries

QU He-Zhi, DU Shan-Shan, HAO Dong-Yun, ZHANG Lei, HUANG Lu, WANG Xiao-Ping*   

  1. Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun 130021, China
  • Received:2007-09-28 Revised:1900-01-01 Online:2008-07-10 Published:2008-07-10
  • Contact: WANG Xiao-Ping

Abstract: CuZn Superoxide dismutase(CuZn-SOD) is the enzyme that can catalyze the removal of superoxide radicals, which are generated in a variety of biological oxidations. It is a ubiquitous enzyme and provides a defense against oxygen toxicity. To dismutate superoxide radical effectively in and around vascular endothelial cells, we constructed a fusion gene encoding a hybrid SOD(namely HBSOD) consisting of human CuZnSOD and a C-terminal basic peptide that binds to heparin-like proteoglycans. The fusion gene was expressed successfully in pichia pastries. The purified HBSOD exhibited a normal SOD activity. The protein also possessed a high binding affinity to heparin proteoglycans.

Key words: Human CuZn superoxide dismutase, Heparin-affinity, Molecular modification, Engineering enzyme

CLC Number: 

TrendMD: