NDLI: The molecular characterization of a catalase from Chinese mitten crab Eriocheir sinensis.

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The molecular characterization of a catalase from Chinese mitten crab Eriocheir sinensis.

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The molecular characterization of a catalase from Chinese mitten crab Eriocheir sinensis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wang, M. Wang, L. Zhou, Z. Gao, Y. Shi, X. Gai, Y. Mu, C. Song, L.
Description	Country affiliation: China Author Affiliation: Wang M ( Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, China.)
Abstract	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 224 bp, a 3' UTR of 1287 bp with a poly (A) tail and an open reading frame (ORF) of 1542 bp, which encoded a polypeptide of 513 amino acid residues with a calculated molecular mass of approximately 58.86 kDa and a theoretical isoelectric point of 6.880. The deduced amino acid sequence of EsCAT contained a highly conserved proximal active-site signature motif ((60)FDRERIPERVVHAKGAL(76)) and a proximal heme-ligand signature motif ((350)RLFSYNDTH(358)) 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 48 h 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.
File Format	HTM / HTML
ISSN	17443121
Issue Number	3
Volume Number	40
e-ISSN	1744313X
Journal	International Journal of Immunogenetics
Language	English
Publisher	Wiley-Blackwell
Publisher Date	2013-06-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Genetics Discipline Immunology Brachyura Enzymology Genetics Catalase Amino Acid Sequence Animals Base Sequence Immunology Microbiology Chemistry Metabolism Dna, Complementary Enzyme Activation Gene Expression Hemocytes Hydrogen-ion Concentration Molecular Sequence Data Organ Specificity Phylogeny Rna, Messenger Sequence Alignment Temperature Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Genetics Molecular Biology Immunology Genetics (clinical)

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