Chem. J. Chinese Universities
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QU He-Zhi, DU Shan-Shan, HAO Dong-Yun, ZHANG Lei, HUANG Lu, WANG Xiao-Ping*
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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:
Q784
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QU He-Zhi, DU Shan-Shan, HAO Dong-Yun, ZHANG Lei, HUANG Lu, WANG Xiao-Ping*. Molecular Modification and Expression of Human CuZn Superoxide Dismutase in pichia pastries[J]. Chem. J. Chinese Universities, doi: .
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URL: http://www.cjcu.jlu.edu.cn/EN/
http://www.cjcu.jlu.edu.cn/EN/Y2008/V29/I7/1390