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¹ Bingöl University, Faculty of Agriculture, Department of Fisheries, 12000-Bingöl, Turkey
² Bingöl University, Faculty of Arts and Science, Department of Chemistry, 12000-Bingöl, Turkey
³ Atatürk University, Faculty of Science, Department of Chemistry, 25240-Erzurum, Turkey
⁴ Atatürk University, Faculty of Fisheries, 25240-Erzurum, Turkey DOI : 10.4194/1303-2712-v16_1_17 Viewed : 3841 - Downloaded : 2927 In this study, in vitroeffects of some metal ions(Fe³⁺, Cd²⁺, Pb²⁺ and Ni²⁺)on cytoplasmic carbonic anhydrase(CA, EC 4.2.1.1) from Capoeta umbla gill was investigated. CA was purified from the gills of C. umbla for the first time. It was purified with the Sepharose-4B-L-Tyrosine Sulphanilamide affinity chromatography method. The overall purification was approx. 31.69-fold with a yield of 53.33%, and a specific activity of 326.73 EU/mg proteins. Sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS-PAGE) showed a single band corresponding to a molecular weight of approx. 29 kDa. The constants of the enzyme inhibitor complex (Ki) and 50% inhibitory values (IC50) for metal ions were determined by Lineweaver-Burk graphs and plotting activity % vs. [I], respectively. The Kiconstants and IC50 values were 0.012±0.0135 and 0.136 mM for Fe³⁺, 0.019±0.0113 and 0.191 mM for Cd²⁺, 0.041±0.0075 and 0.289 mM for Pb²⁺, and 0,120±0.034 and 0.924 mM for Ni²⁺. It was determined that Fe³⁺, Cd²⁺ and Pb²⁺ inhibited the enzyme competitively while Ni²⁺ inhibited the enzyme noncompetitively. The potential inhibitor for C. umbla gill CA was found as Fe³⁺ from these results. Keywords : Capoeta umbla, carbonic anhydrase, gills, metal toxicity