Sürdürülebilir Kalkınma Amaçları
Yayınlar
- MakaleYalnız künye2018Evaluation of Inhibition Effects of Some Cardiovascular Therapeutics on Human Erythrocyte Carbonic Anhydrase Isoenzymes
Isgor, Mehmet Mustafa; Kılınç, Namık; Alim, Zuhal; Beydemir, Şükrü; Sengül, Bülent
Carbonic anhydrase enzyme plays a vital role in metabolic events such as acid-base regulation and respiration. Inour research, it is tried to determine the inhibitory influences of the cardiovascular therapeutics esmololhydrochloride, amiodarone hydrochloride and lidocaine hydrochloride on human erythrocytes carbonic anhydrases(hCA I and II). In accordance with this purpose, carbonic anhydrase isoenzymes were purified from humanerythrocytes by using affinity chromatography method. Enzyme purity was checked by SDS-PAGEelectrophoresis method. After the carbonic anhydrase enzymes were purified, the inhibitory affects ofcardiovascular therapeutics on these enzymes, using esterase activity, which is the method of measuring in vitroactivity, were examined. The three cardiovascular therapeutics dose-dependently decreased activity of hCAs. IC50values of amiodarone hydrochloride, esmolol hydrochloride and lidocaine hydrochloride were found to be,respectively, 0.91 mM, 5 mM, 5.8 mM for hCA-I and 0.41 mM, 3.5 mM, and 6.36 mM for hCA-II. Our resultsproved that, under in vitro conditions, cardiovascular therapeutics significantly inhibit human CA-I and IIactivities. So, irregular use of these medicines may cause serious adverse effects in terms of human health.
AtıfTR Dizin2
İncele - MakaleYalnız künye2018Scopus SJRQ2The interactions of cephalosporins on polyol pathway enzymes from sheep kidney
Şengül, Bülent; Beydemir, Şükrü
Context: Cephalosporins are derived from the fungus Acremonium. Due to their strong bactericidal ability, these drugs have to a wide usage in medicine. Objective: An investigation of the effects on sheep renal aldose reductase (AR) and sorbitol dehydrogenase (SDH) of cefoperazone, cefazolin, cefuroxime, ceftazidime and ceftriaxone as cephalosporin drugs was carried out in the present study. Methods: AR and SDH were purified from sheep kidney by ion exchange, gel filtration and affinity methods with approximately 219- and 484-fold, respectively. Some kinetic properties of the enzymes were determined such as optimal pH, optimal ionic strength, optimal temperature, stable pH, Km and Vmax. IC50 values of the drugs were found for each enzyme. Results: While the AR was inhibited by all drugs, SDH enzyme was inhibited by only CXM (IC50 8.10 mM). Interestingly, CZO activated SDH enzyme. This result was evaluated as important for the flow of the polyol reactions. Ki values and inhibition types were determined for AR. However, these values could not have determined for SDH, due to insufficient inhibition. Conclusions: From these results, it was concluded that cephalosporins may have an important effect on flow of the polyol metabolism.
AtıfScopus12WoS12OpenAlex13
İncele - MakaleYalnız künye2017Alcohol Dehydrogenase from Sheep Liver: Purification, Characterization and Impacts of Some Antibiotics
Demir, Yeliz; Ergun, Bülent; Beydemir, Şükrü; Sengül, Bülent
Alcohol dehydrogenase (ADH) is a dimeric enzyme in which each subunit of the enzyme has a Zn2+metal-containing catalytic domain and a cofactor-binding domain. This enzyme converts the alcohol to aldehyde. The present article focuses on the purification, characterization and in vitro effects of some antibiotics on alcohol dehydrogenase from sheep liver. ADH was purified with specific activity of 0.5 U/mg proteins and approximately 52.03-fold from sheep liver by DEAE-Sephadex A-50 ion exchange chromatography and gel filtration on Sephadex G-100. The subunit and the natural molecular weights of the enzyme were determined by gel filtration and SDSPAGE 38.16 kDa and 80.49 kDa, respectively. The optimum ionic strenght, temperature and pH of ADH were found 400 mM, 40 °C and 10.5, respectively. The inhibitory effects of the antibiotics were tested at various concentrations. IC values for kanamycin sulfate, amikacin sulfate, gentamicin, lincomycin, and clindamycin were found to be 43.31, 36.47, 20.38, 18.73 and 1.31 mM, respectively
AtıfTR Dizin2İncele - MakaleAçık Erişim2017Scopus SJRQ1Inhibition behaviours of some phenolic acids on rat kidney aldose reductase enzyme: an in vitro study
Alim, Zuhal; Kilinç, Namik; Şengül, Bülent; Beydemir, Şükrü
Aldose reductase (AR) inhibitors have vital importance in the treatment and prevention of diabetic complications. In this study, rat kidney AR was purified 19.34-fold with a yield of 3.49% and a specific activity of 0.88 U/mg using DE-52 Cellulose anion exchange chromatography, gel filtration chromatography and 2′5′ ADP Sepharose-4B affinity chromatography, respectively. After purification, the in vitro inhibition effects of some phenolic acids (tannic acid, chlorogenic acid, sinapic acid, protocatechuic acid, 4-hydroxybenzoic acid, p-coumaric acid, ferulic acid, vanillic acid, syringic acid, α-resorcylic acid, 3-hydroxybenzoic acid and gallic acid) were investigated on purified enzyme. We determined IC50, Ki values and inhibition types of these phenolic acids. As a result, tannic and chlorogenic acid had a strong inhibition effect. On the other hand, gallic acid had a weak inhibition effect. In this study, all phenolic acids except for chlorogenic acid and p-coumaric acid showed non-competitive inhibition effects on rat kidney AR.
AtıfScopus61WoS60OpenAlex64İncele - MakaleYalnız künye2016Scopus SJRQ2In vitro inhibitory effects of palonosetron hydrochloride, bevacizumab and cyclophosphamide on purified paraoxonase-I (hPON1) from human serum
Türkeş, Cüneyt; Söyüt, Hakan; Beydemir, Şükrü
In this study, we investigated the effects of the drugs, palonosetron hydrochloride, bevacizumab and cyclophosphamide, on human serum paraoxonase-I (hPON1) enzyme activity in in vitro conditions. The enzyme was purified ~231-fold with 34.2% yield by using ammonium sulphate precipitation, DEAE-Sephadex A-50 ion-exchange chromatography and Sephadex G-200 gel-filtration chromatography from human serum. hPON1 exhibited a single protein band on the SDS polyacrylamide gel electrophoresis. The inhibition studies were performed on paraoxonase activity of palonosetron hydrochloride, bevacizumab and cyclophosphamide. Ki constants were found as 0.033 ± 0.001, 0.054 ± 0.003 mM and 3.419 ± 0.518 mM, respectively. Compared to the inhibition rates of the drugs, palonosetron hydrochloride has the maximum inhibition rate. However, inhibition mechanisms of the drugs were determined as noncompetitive by Lineweaver-Burk curves.
AtıfScopus49WoS49OpenAlex56İncele - 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.
AtıfScopus17WoS16OpenAlex19İncele - MakaleYayıncıda açık erişim2015Scopus SJRQ1Human serum paraoxonase-1 (hPON1): In vitro inhibition effects of moxifloxacin hydrochloride, levofloxacin hemihidrate, cefepime hydrochloride, cefotaxime sodium and ceftizoxime sodium
Türkeş, Cüneyt; Söyüt, Hakan; Beydemir, Şükrü
In this study, we investigated the effects of antibacterial drugs (moxifloxacin hydrochloride, levofloxacin hemihidrate, cefepime hydrochloride, cefotaxime sodium and ceftizoxime sodium) on human serum paraoxonase-1 (hPON1) enzyme activity from human serum in vitro conditions. For this purpose, hPON1 enzyme was purified from human serum using simple chromatographic methods. The antibacterial drugs exhibited inhibitory effects on hPON1 at low concentrations. Ki constants were calculated to be 2.641 ± 0.040 mM, 5.525 ± 0.817 mM, 35.092 ± 1.093 mM, 252.762 ± 5.749 mM and 499.244 ± 10.149 mM, respectively. The inhibition mechanism of moxifloxacin hydrochloride was competitive, whereas levofloxacin hemihidrate, cefepime hydrochloride, cefotaxime sodium and ceftizoxime sodium were noncompetitive inhibitors.
AtıfScopus53WoS53OpenAlex57İncele - MakaleAçık Erişim2014Scopus SJRQ2Impact of antibacterial drugs on human serum paraoxonase-1 (hPON1) activity: An in vitro study
Söyüt, Hakan; Kaya, Elif Duygu; Beydemir, Şükrü
Objective: To investigate the in vitro effects of the antibacterial drugs, meropenem trihydrate, piperacillin sodium, and cefoperazone sodium, on the activity of human serum paraoxonase (hPON1). Methods: hPON1 was purified from human serum using simple chromatographic methods, including DEAE-Sephadex anion exchange and Sephadex G-200 gel filtration chromatography. Results: The three antibacterial drugs decreased in vitro hPON1 activity. Inhibition mechanisms meropenem trihydrate was noncompetitive while piperacillin sodium and cefoperazone sodium were competitive. Conclusions: Our results showed that antibacterial drugs significantly inhibit hPON1 activity, both in vitro, with rank order meropenem trihydrate piperacillin sodium cefoperazone sodium in vitro.
AtıfScopus5OpenAlex7İncele - MakaleAçık Erişim2014Scopus SJRQ2Effect of calcium channel blockers on paraoxonase-1 (PON1) activity and oxidative stress
Türkeş, Cüneyt; Söyüt, Hakan; Beydemir, Şükrü
Background: In this study, we investigated the in vitro effects of calcium channel blockers (nifedipine, nitrendipine, isradipine, and amlodipine besylate) on the activity of paraoxonase-1 (PON1). Methods: PON1 was purified from human serum using simple chromatographic methods, including DEAE-Sephadex anion-exchange and Sephadex G-200 gel filtration chromatography. Results: The calcium channel blockers decreased the in vitro PON1 activity. The inhibition mechanism of amlodipine besylate was noncompetitive, whereas nifedipine, nitrendipine, and isradipine were competitive inhibitors. Conclusions: Our results showed that calcium channel blockers exhibit inhibitory effects on PON1 at low concentrations. The IC50 values for nifedipine, nitrendipine, isradipine, and amlodipine besylate were determined to be 0.121 mM, 0.130 mM, 0.255 mM, and 0.304 mM, respectively, and the Ki constants were calculated to be 0.222 ± 0.049 mM, 0.151 ± 0.067 mM, 0.286 ± 0.137 mM, and 0.321 ± 0.002 mM, respectively.
AtıfScopus68WoS67OpenAlex74İncele - 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