期刊
INTERNATIONAL JOURNAL OF IMMUNOGENETICS
卷 40, 期 3, 页码 230-240出版社
WILEY
DOI: 10.1111/iji.12019
关键词
-
资金
- National Basic Research Program of China (973 program) [2012CB114405]
- Shandong Provincial Natural Science Foundation, China [JQ201110]
Catalase (CAT) is an antioxidant enzyme and plays a significant role in the protection against oxidative stress by reducing hydrogen peroxide. The CAT cDNA of Eriocheir sinensis (EsCAT) was cloned via RACE technique. The complete sequence of EsCAT cDNA consisted of a 5 untranslated regions (UTR) of 224bp, a 3 UTR of 1287bp with a poly (A) tail and an open reading frame (ORF) of 1542bp, which encoded a polypeptide of 513 amino acid residues with a calculated molecular mass of approximately 58.86kDa and a theoretical isoelectric point of 6.880. The deduced amino acid sequence of EsCAT contained a highly conserved proximal active-site signature motif (60FDRERIPERVVHAKGAL76) and a proximal hemeligand signature motif (350RLFSYNDTH358) and exhibited high similarity with other reported CATs. In the phylogenetic tree, EsCAT was clustered with the CATs from Scylla serrata and Portunus trituberculatus. The EsCAT transcripts were constitutively expressed in haepatopancreas, haemocytes, gill, gonad, muscle and heart, with highest expression level in haepatopancreas. The relative expression level of EsCAT mRNA in haemocytes was continuously up-regulated and reached the peak level at 48h post-Vibrio anguillarum challenge. The purified recombinant EsCAT protein displayed antioxidant activity against hydrogen peroxide with high thermal stability and broad spectrum of pH values. All these results demonstrated that EsCAT was an efficient antioxidant enzyme and potentially involved in the regulation of redox and innate immune response of crabs.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据