ANIMAL BIOTECHNOLOGY, cilt.34, sa.8, ss.3578-3588, 2023 (SCI-Expanded)
The aim of this study is to determine the effects of 50% of 96h LC50(5.25ppm) diazinon onthe expression of superoxide dismutase (SOD) enzyme genes (sod1,sod2, andsod3b) andSOD enzyme activity at the end of 24, 48, 72, and 96 h in platyfish liver and gill tissues. Tothis end, we determined the tissue-specific distribution ofsod1,sod2, andsod3bgenes andperformedin silicoanalyses in platyfish (Xiphophorus maculatus). It was determined thatmalondialdehyde (MDA) level and SOD enzyme activity were increased in the liver [(43.90EU mg protein1(control), 62.45 EU mg protein1(24 h), 73.17 EU mg protein1(48 h),82.18 EU mg protein1(72h), 92.93 EU mg protein1(96 h)] and gill [(16.44 EU mgprotein1(control), 33.47 EU mg protein1(24h), 50.38 EU mg protein1(48h), 64.62 EUmg protein1(72h), 74.04 EU mg protein1(96h)] tissues of platyfish exposed to diazinon,while the expression of thesodgenes was down-regulated. The tissue-specific distributionof thesodgenes varied, with the tissues and thesodgenes expression were being predom-inant in the liver (628.32 insod1, 637.59 insod2, 888.5 insod3b). Thus, the liver was consid-ered a suitable tissue for further gene expression studies. Based on the phylogeneticanalyses, platyfishsodgenes can be reported to be orthologs ofsod/SODgenes from othervertebrates. Identity/similarity analyses supported this determination. Conserved gene syn-teny proved that there are conservedsodgenes in platyfish, zebrafish, and humans