人过氧化氢酶基因的克隆与表达  

Cloning and expression of human catalase gene in E. coli

作　　者：耿风廷[1] 赵晓瑜[1] 高珊[1] 

机构地区：[1]河北大学生命科学学院,河北保定071002

出　　处：《中国生化药物杂志》2007年第3期188-191,共4页Chinese Journal of Biochemical Pharmaceutics

摘　　要：目的利用基因重组技术在大肠杆菌中高效表达人过氧化氢酶(catalase,CAT)。方法从人cDNA文库中获得CAT编码基因,并利用pMAL-c2x、pBV221质粒分别构建了融合和非融合表达载体并进行了表达和活性检测。结果融合表达与非融合表达均可获得可溶性蛋白质,非融合的表达产物具有CAT活性,而融合表达产物在切除融合蛋白质(MBP)部分后表现出明显的CAT活性。结论从大肠杆菌表达体系能表达具有生物活性的CAT,此项研究为后续重组酶性质的研究和开发利用奠定了基础。To produce human catalase （CAT）on a large scale in E. coli by recombinant DNA technology, CAT gene was obtained by PCR from the human eDNA library, and the expression vectors were constructed by using two different plasmids （pMAL-c2x and pBV221 ） and transformed into E. coli. The expressed products of the two reeombinants were soluble. The expressed protein of pBV-CAT had the biological activity of CAT, but the expressed fusion protein of pMAL-c2x-CAT didn＇t have the activity unless the MBP was removed from the fusion protein. So recombinant human CAT having biological activity can be obtained from E. coli expression system. This is the basis of the future study and application of the recombinant proteins.

关 键 词：人过氧化氢酶基因 大肠杆菌 表达 融合表达 

分 类 号：Q785[生物学—分子生物学] Q786