A fused selenium-containing protein with both GPx and SOD activities

被引:46
作者
Yu, Huijun
Ge, Yan
Wang, Ying
Lin, Chi-Tsai
Li, Jing
Liu, Xiaoman
Zang, Tianzhu
Xu, Jiayun
Liu, Junqiu [1 ]
Luo, Guimin
Shen, Jiacong
机构
[1] Jilin Univ, Key Lab Supramol Struct & Mat, Minist Educ, Changchun 130012, Peoples R China
[2] Natl Taiwan Ocean Univ, Inst Marine Biotechnol, Chilung 2024, Taiwan
[3] Jilin Univ, Key Lab Mol Enzymol & Engn, Minist Educ, Changchun 130023, Peoples R China
基金
中国国家自然科学基金;
关键词
bifunctional enzyme; artificial enzymes; fusion protein; glutathione peroxidase; selenium-containing glutathione transferase; superoxide dismutase;
D O I
10.1016/j.bbrc.2007.05.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
As a safeguard against oxidative stress, the balance between the main antioxidant enzymes including superoxide dismutase (SOD), glutathione peroxidase (GPx), and catalase (CAT) was believed to be more important than any single one, for example, dual-functional SOD/CAT enzyme has been proved to have better antioxidant ability than either single enzyme. By combining traditional fusion protein technology with amino acid auxotrophic expression system, we generated a bifunctional enzyme with both GPx and SOD activities. It displayed better antioxidant ability than GPx or SOD. Such dual-functional enzymes could facilitate further studies of the cooperation of GPx and SOD and generation of better therapeutic agents. (C) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码:873 / 878
页数:6
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