Abstract
Abstract CuZn–superoxide dismutase (CuZn–SOD) is a key antioxidant enzyme playing a first line protective role against reactive oxygen species (ROS) by converting superoxide () into H2O2. The CuZn–SOD gene was isolated from a whole abalone cDNA library and denoted as aCuZn–SOD. The full‐length cDNA of aCuZn–SOD was 1021 bp, which contained 465‐bp open reading frame (ORF) coding 154 amino acids. It contained highly conserved CuZn–SOD signature motif 1 (45GFHVHQFGDNT55) and motif 2 (139GNAGGRQACGVI150). Also, amino acid residues identified as Cu (His47, His49, His64, and His121) and Zn (His64, His72, His81, and ASP84) metal‐binding sites were completely conserved in the aCuZn–SOD. The reverse transcription polymerase chain reaction (RT‐PCR) results showed that aCuZn–SOD mRNA was expressed constitutively in gill, mantle, gonad, abductor muscle, digestive tract, and hemocytes in a tissue‐specific manner. The aCuZn–SOD mRNA was significantly up‐regulated (P < 0.05) in gill and digestive tract tissues after Aroclor 1254 induction compared to untreated and methanol‐injected abalone groups, suggesting that abalone has a potential use in assessing the impact of marine pollutants with the application of gene expression concept. In addition, purified recombinant aCuZn–SOD fusion protein was shown to reduceradical generated by xanthine oxidase assay, showing CuZn–SOD is a functionally active antioxidant enzyme in disk abalone.
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