Sürdürülebilir Kalkınma Amaçları
Yazarlar
- Söyüt, Hakan(4)
- Kaya, Elif Duygu(3)
- Beydemir, Şükrü(2)
- Demir, Nazan(2)
- Demir, Yasar(2)
- Tasgin, Esen(2)
- Balaydiin, Halis Türker(1)
- Beydemir, Sukru(1)
- Beydemir, Sükrü(1)
- Beydemir, Şkrü(1)
- Ceyhun, Saltuk Buǧrahan(1)
- Coskun, Fatma(1)
- Ekinci, Deniz(1)
- Erdoǧan, Orhan(1)
- Göksu, Sleyman(1)
- Menzek, Abdullah(1)
- Nadaroglu, Hayrunnisa(1)
- Soyut, Hakan(1)
- Şahin, Ertan(1)
Yayınlar
- MakaleAçık Erişim2015Scopus SJRQ2The toxicological impacts of some heavy metals on carbonic anhydrase from gilthead sea bream (Sparus aurata) gills
Kaya, Elif Duygu; Söyüt, Hakan; Beydemir, Şükrü
It is known that heavy metals have toxic effects on fish. Insufficient measures are a serious problem in our country and around the world. This problem can threaten human health in areas where it is common for people to obtain nutrition from local bodies of water. In this study, the toxicological impacts of some heavy metals were investigated on carbonic anhydrase activity in gilthead gills. Carbonic anhydrase (CA) was purified from gilthead sea bream (Sparus aurata) gills with a specific activity of 2872.92EUmg-1 and a yield of 32.84% using affinity chromatography. The overall purification was approximately ~84-fold. SDS-polyacrylamide gel electrophoresis showed a single band, and the MW was approximately 30.5kDa (Soyut et al., 2008, 2012; Soyut and Beydemir, 2008, 2012; Kaya et al., 2013). The kinetic and characteristic properties of CA such as the optimum pH, stable pH, optimum temperature, activation energy (Ea), activation enthalpy (δH), Q10, Km and Vmax were determined. Cadmium (Cd2+), copper (Cu2+), nickel (Ni2+) and silver (Ag+) inhibited CA activity in in vitro conditions. Ki values were calculated for these metals. Ki values were 31.20mM for cadmium (Cd2+), 161.96mM for copper (Cu2+), 10.79mM for nickel (Ni2+) and 0.0082mM for silver (Ag+) based on Lineweaver-Burk plots. Except for cadmium, heavy metals had the same inhibition mechanism. Cadmium was competitive, and the others were noncompetitive.
AtıfScopus17WoS16OpenAlex19
İncele - MakaleAçık Erişim2013Scopus SJRQ2Carbonic anhydrase activity from the gilthead sea bream (Sparus aurata) liver: The toxicological effects of heavy metals
Kaya, Elif Duygu; Söyüt, Hakan; Beydemir, Sukru
Many studies have shown that metal ions may lead to oxidative stress in biological systems. Accordingly, DNA damage, protein modification, enzyme inhibition and activation, lipid peroxidation and many other effects may occur in living organisms. Many different formations of metal ions may enter human cells along with water, air, and various foods, and humans are negatively affected by these conditions, either directly or indirectly. These effects may cause irreversible damage to human metabolism. In this study, the toxicological effects of heavy metals on carbonic anhydrase enzyme activity from the gilthead sea bream liver were investigated. The carbonic anhydrase enzyme was purified via affinity chromatography and had a specific activity of 6775.5 EU mg(-1). The kinetics and characteristic properties, such as optimum pH, stable pH, optimum temperature, activation energy (E-a), activation enthalpy (Delta H), Q(10), K-m, and V-max, were determined for the purified enzyme SDS-polyacrylamide gel electrophoresis showed a single band and molecular weight of the subunit was approximately 25 kDa. Cd(II), Cu(II), Ni(II) and Ag(I) inhibited the enzyme activity in vitro. The type of inhibition and K-i values for these metals were calculated from Lineweaver-Burk plots as 17.74 mM, 36.20 mM, 12.85 mM and 0.025 mM for Cd(II), Cu(II), Ni(II) and Ag(I), respectively. All the metals were noncompetitive inhibitors. (C) 2013 The Authors. Published by Elsevier B.V. All rights reserved.
AtıfWoS27OpenAlex32İncele - MakaleYalnız künye2012Scopus SJRQ4Expression of cytosolic and noncytosolic carbonic anhydrase enzymes from bovine brain membrane
Demir, Nazan; Demir, Yasar; Coskun, Fatma; Tasgin, Esen
Carbonic anhydrase is an enzyme that takes responsibility in inhalation function but, until today, carbonic anhydrase is not examined if it is present in the bovine brain membrane or not. The enzyme carbonic anhydrase was purified and separately characterized according to the bonding forms in 4 steps such as outer peripheral, cytosolic, inner peripheral and integral. Affinity chromatography was used for purification of the enzyme in all four steps. The affinity column was prepared with sepharose-4B-L-tyrosine-sulphanilamide. Purified carbonic anhydrase was obtained at each step. Enzyme activity was measured by CO2 hydratase activity and esterase activity methods. Optimum pH and optimum temperature were defined for purified enzymes at each step. Morover molecular weight and purity were detected by gel filtration and SDS-PAGE electrophorose. In addition, the enzyme's Km and nmax values were found with the Lineweaver- Burk method. The obtained results are discussed in comparison with other mammalian carbonic anhydrases. Carbonic anhydrase was shown to be exist in bovine brain membrane and this enzyme was optimized.
AtıfScopus1İncele - MakaleAçık Erişim2012Scopus SJRQ3Changes in carbonic anhydrase activity and gene expression of Hsp70 in rainbow trout (Oncorhynchus mykiss) muscle after exposure to some metals
Söyüt, Hakan; Beydemir, Sükrü; Ceyhun, Saltuk Buǧrahan; Erdoǧan, Orhan; Kaya, Elif Duygu
The effects of some heavy metals Co(II), Cu(II), Zn(II), and Ag(I) on carbonic anhydrase (CA) activity from rainbow trout (RT) muscle were investigated. Moreover, the effects of these metals on the expression of heat shock protein 70 (Hsp70) gene in muscle tissue were examined by real-time quantitative PCR (RT-PCR) in muscle tissue aft er exposure to the metals at the end of 6, 12, 24, and 48 h. CA was purified with a specific activity of 2300 EU mg-1, a yield of 19%, and 1080-fold. The molecular weights (Mw) of subunit and native enzyme were approximately 30 and 31 kDa, respectively. Optimum pH, stable pH, optimum temperature, activation energy (Eα), activation enthalpy (ΔH), and Q10 (the difference in activity of enzyme caused by the increment of 10 oC) value were determined. Apparent Michaelis constant (Km), maximum reaction rate (Vmax), and turnover rate of the enzyme (Kcat) values were 1.29 mM, 0.17 μmol min-1, and 28.8 s-1, respectively. The catalytic efficiency (Kcat/Km) was 22.3. The heavy metals decreased in vitro CA activity. Inhibition mechanisms of the metal ions were noncompetitive, except for the Co(II) ion, which was competitive. The expression of the Hsp70 gene was increased in the presence of the metal ions. The expression level at the end of 48 h was the highest for all of the metals. Consequently, the in vitro inhibition rank order was determined as Co(II) > Zn(II) > Cu(II) > Ag(I). Interestingly, Ag(I) was the most effective metal ion on Hsp70 gene expression.
AtıfScopus9WoS8OpenAlex9İncele - MakaleAçık Erişim2012Scopus SJRQ2The impact of heavy metals on the activity of carbonic anhydrase from rainbow trout (Oncorhynchus mykiss) kidney
Söyüt, Hakan; Beydemir, Şükrü
Many environmental and health problems have become a consequence of contamination of soil and water by toxic heavy metals and organic pollutants in the present age of technology. Heavy metals play vital roles in enzyme activities and other metabolic events with their bioaccumulative and nonbiodegradable properties among aquatic pollutants. Metal toxicity causes irregular metallothioneins protein synthesis, renal damage, and disruption of bone structure in humans and wildlife. In this study, we investigated in vitro effects of some metals on chemical-targeted carbonic anhydrase (CA) enzyme from rainbow trout kidney. The enzyme was purified with a specific activity of 17,285 EU × mg-1 and 31.7% yield and approximately 1800-fold using simple affinity purification method. Molecular weights of the subunit and native enzyme were estimated as 28.7 kDa and 26.9 kDa via sodium dodecyl sulfate polyacrylamide gel electrophoresis and Sephadex-G 200 column, respectively. Other kinetic properties of the enzyme were determined. Apparent Km, Vmax and kcat values were 0.40 mM, 0.097 μmol min-1 and 15.2 s-1 for p-nitrophenylacetate substrate, respectively. Inhibitory effects of cobalt, zinc, copper, cadmium and silver on CA activity were determined using the esterase method under in vitro conditions. IC50 and Ki values were calculated for metals. Ki values for Co2+, Zn2+, Cu2+, Cd2+ and Ag+ were 0.035, 1.2, 34.8, 103 and 257 from Lineweaver-Burk graphs, respectively. Consequently, in vitro inhibition rank order was determined as Co2+ > Zn2+ > Cu 2+ > Cd2+ > Ag+. The potential inhibitor for CA was found as Co2+ from these results.
AtıfScopus17WoS17OpenAlex17İncele - MakaleAçık Erişim2012Scopus SJRQ2Synthesis and carbonic anhydrase inhibitory properties of novel bromophenols including natural products
Balaydiin, Halis Türker; Soyut, Hakan; Ekinci, Deniz; Göksu, Sleyman; Beydemir, Şkrü; Menzek, Abdullah; Şahin, Ertan
(2-Bromo-3,4-dimethoxyphenyl) (3,4-dimethoxyphenyl)methanone (10) and its derivatives with Br, one dibromide and isomeric three tribromides, were synthesized. Demethylation of these compounds afforded a series of new bromophenols. Inhibition of human cytosolic carbonic anhydrase II (hCA II) isozyme by these new bromophenols and naturally occurring 3,4,6-tribromo-5-(2,5- dibromo-3,4-dihydroxybenzyl)benzene-1,2-diol (3), and 5,5′-methylenebis(3, 4,6-tribromo-benzene-1,2-diol) (4) was investigated. The synthesized compounds showed carbonic anhydrase inhibitory capacities with IC 50 values in the range of 0.7372 μM against hCA II. Some bromophenols investigated here showed effective hCA II inhibitory activity and might be used as leads for generating novel carbonic anhydrase inhibitors which are valuable drug candidates for the treatment of glaucoma, epilepsy, gastric and duodenal ulcers, neurological disorders, or osteoporosis.
AtıfScopus42WoS43OpenAlex41İncele - MakaleYalnız künye2009Scopus SJRQ3Purification and properties of carbonic anhydrase from bone marrow
Tasgin, Esen; Nadaroglu, Hayrunnisa; Demir, Yasar; Demir, Nazan
In this work, the carbonic anhydrase was purified from bovine bone marrow and investigated its kinetic properties. Carbonic anhydrase was purified from bovine bone marrow using affinity chromatography by sepharose 4B-L-tyrosine sulphanilamide. During purification steps, the activity of enzyme was measured using p-nitrophenyl acetate at pH: 7.4. Optimum pH and optimum temperature values for bovine bone marrow carbonic anhydrase were determined and then K m and Vmax values for the same substrate were obtained by means of Linewearver-Burk graphics. The purification degree for bovine bone marrow was calculated. The Vmax, and Km values at optimum pH and at 20 °C for the substrate (p-nitrophenyl acetate) were 120.418 uμmol/L min and 2.409 x 103 mM, respectively. The K1 and I50 values for sulfanilamide, KSCN, NaN3 and acetazolamide were determined in bovine bone marrow carbonic anhydrase.
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