人CuZn-SOD的分子改造及在毕赤酵母中的表达  

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

作　　者：曲和之[1] 杜姗姗[1] 郝东云[1] 张雷[1] 黄露[1] 王晓平[1] 

机构地区：[1]吉林大学分子酶学工程教育部重点实验室,长春130021

出　　处：《高等学校化学学报》2008年第7期1390-1392,共3页Chemical Journal of Chinese Universities

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.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 de- fense 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.

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 

分 类 号：Q784[生物学—分子生物学]