Cloning, characterization and tissue expression of disk abalone (Haliotis discus discus) catalase Export

@article{citeulike:5518923, abstract = {Catalase is an antioxidant enzyme that plays a significant role in protection against oxidative stress by detoxification of hydrogen peroxide (H 2 O 2 ). A gene coding for a putative catalase was isolated from the disk abalone ( Haliotis discus discus ) cDNA library and denoted as Ab-catalase. The full-length (2864 bp) Ab-catalase cDNA contained 1,503 bp open reading frame (ORF), encoding 501 amino acid residues with 56 kDa predicted molecular weight. The deduced amino acid sequence of Ab-catalase has characteristic features of catalase family such as catalytic site motif ( 61 FNRERIPERVVHAKGAG 77 ), heme-ligand signature motif ( 351 RLYSYSDT 358 ), NADPH and heme binding residues. Phylogenetic and pairwise identity results indicated that Ab-catalase is more similar to scallop ( Chlamys farreri ) catalase with 80\% amino acid identity except for other reported disk abalone catalase sequences. Constitutive Ab-catalase expression was detected in gill, mantle, gonad, hemocytes, abductor muscle and digestive tract in tissue specific manner. Ab-catalase mRNA was up-regulated in gill and digestive tract tissues for the first 3 h post injection of H 2 O 2 , showing the inducible ability of abalone catalase against oxidative stress generated by H 2 O 2 . The purified recombinant catalase showed 30,000 U/mg enzymatic activity against H 2 O 2 and biochemical properties of higher thermal stability and broad spectrum of pH. Our results suggest that abalone catalase may play an important role in regulating oxidative stress by scavenging H 2 O 2 .}, author = {Ekanayake, P. and Dezoysa, M. and Kang, H. and Wan, Q. and Jee, Y. and Lee, Y. and Kim, S. and Lee, J.}, citeulike-article-id = {5518923}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.fsi.2007.11.007}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S1050464807001921}, doi = {10.1016/j.fsi.2007.11.007}, issn = {10504648}, journal = {Fish \& Shellfish Immunology}, keywords = {expression, haliotis, protein}, month = {March}, number = {3}, pages = {267--278}, posted-at = {2009-08-21 10:46:44}, priority = {2}, title = {Cloning, characterization and tissue expression of disk abalone (Haliotis discus discus) catalase}, url = {http://dx.doi.org/10.1016/j.fsi.2007.11.007}, volume = {24}, year = {2008} }

TY - JOUR ID - citeulike:5518923 L3 - citeulike-article-id:5518923 N2 - Catalase is an antioxidant enzyme that plays a significant role in protection against oxidative stress by detoxification of hydrogen peroxide (H 2 O 2 ). A gene coding for a putative catalase was isolated from the disk abalone ( Haliotis discus discus ) cDNA library and denoted as Ab-catalase. The full-length (2864 bp) Ab-catalase cDNA contained 1,503 bp open reading frame (ORF), encoding 501 amino acid residues with 56 kDa predicted molecular weight. The deduced amino acid sequence of Ab-catalase has characteristic features of catalase family such as catalytic site motif ( 61 FNRERIPERVVHAKGAG 77 ), heme-ligand signature motif ( 351 RLYSYSDT 358 ), NADPH and heme binding residues. Phylogenetic and pairwise identity results indicated that Ab-catalase is more similar to scallop ( Chlamys farreri ) catalase with 80% amino acid identity except for other reported disk abalone catalase sequences. Constitutive Ab-catalase expression was detected in gill, mantle, gonad, hemocytes, abductor muscle and digestive tract in tissue specific manner. Ab-catalase mRNA was up-regulated in gill and digestive tract tissues for the first 3 h post injection of H 2 O 2 , showing the inducible ability of abalone catalase against oxidative stress generated by H 2 O 2 . The purified recombinant catalase showed 30,000 U/mg enzymatic activity against H 2 O 2 and biochemical properties of higher thermal stability and broad spectrum of pH. Our results suggest that abalone catalase may play an important role in regulating oxidative stress by scavenging H 2 O 2 . IS - 3 JF - Fish & Shellfish Immunology SN - 10504648 EP - 278 TI - Cloning, characterization and tissue expression of disk abalone (Haliotis discus discus) catalase VL - 24 SP - 267 KW - expression KW - haliotis KW - protein AU - Ekanayake, P AU - Dezoysa, M AU - Kang, H AU - Wan, Q AU - Jee, Y AU - Lee, Y AU - Kim, S AU - Lee, J PY - 2008/03// UR - http://dx.doi.org/10.1016/j.fsi.2007.11.007 ER -