Inhibitory properties of some heavy metals on carbonic anhydrase I and II isozymes activities purified from Van Lake fish (<Emphasis Type="Italic">Chalcalburnus Tarichi</Emphasis>) gill |
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| Authors: | Müslüm Kuzu Veysel Çomakl? Ebru Akkemik Mehmet Çiftci Ömer ?rfan Küfrevio?lu |
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| Institution: | 1.Faculty of Pharmacy,University of A?r? ?brahim ?e?en,A?r?,Turkey;2.School of Healthy,University of A?r? ?brahim ?e?en,A?r?,Turkey;3.Faculty of Engineering and Architecture,Siirt University,Siirt,Turkey;4.Faculty of Science and Letters,Bing?l University,Bing?l,Turkey;5.Faculty of Science,Atatürk University,Erzurum,Turkey |
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| Abstract: | In this study, CA I and II isoenzymes were purified from Van Lake fish gills by using Sepharose-4B-L-tyrosine-sulfanilamide affinity chromatography and to determine the effects of some metals on the enzyme activities. For purified CA I isoenzyme, yield, specific activity, and purification fold were obtained as 42.07%, 4948.12 EU/mg protein, and 116.61 and for CA II isoenzyme, 7%, 1798.56 EU/mg protein, and 42.38 respectively. Activity of CA was determined by measuring “CO2-hydratase activity”. Purity control was checked by SDS-PAGE. In vitro inhibitory effect of Cu2+, Ag+, Cd2+, Ni2+ metal ions, and arsenic (V) oxide were also examined for both isozymes activities. Whereas Cu2+, Ag+, Cd2+, and Ni2+ ions showed inhibitory effects on both isozymes, arsenic (V) oxide showed activation effect. IC50 values were calculated by drawing activity %-I] graphs for metal ions exhibiting inhibitory effects. IC50 values were determined as 3.39, 6.38, 13.52, and 206 μM for CA I isozyme and 6.16, 20.29, 46, and 223 μM for CA II isozyme respectively. |
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