人CuZn-SOD的分子改造及在毕赤酵母中的表达

高等学校化学学报

人CuZn-SOD的分子改造及在毕赤酵母中的表达

曲和之, 杜姗姗, 郝东云, 张雷, 黄露, 王晓平

吉林大学分子酶学工程教育部重点实验室, 长春 130021

收稿日期:2007-09-28 修回日期:1900-01-01 出版日期:2008-07-10 发布日期:2008-07-10
通讯作者: 王晓平

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*

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

摘要/Abstract

摘要： 为了改善人CuZn-SOD的酶学性质, 在借鉴人细胞外超氧化物歧化酶的特性基础上, 利用分子生物学技术, 在人CuZn-SOD的C末端加入肝素亲和肽构建了人CuZn-SOD工程酶, 并在毕赤酵母中获得表达, 经纯化的工程酶具有较强的肝素亲和性.

关键词: 人铜锌超氧化物歧化酶, 肝素亲和性, 分子改造, 工程酶

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

中图分类号:

Q784

TrendMD:

曲和之, 杜姗姗, 郝东云, 张雷, 黄露, 王晓平. 人CuZn-SOD的分子改造及在毕赤酵母中的表达. 高等学校化学学报, doi: .

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. Chem. J. Chinese Universities, doi: .