Sürdürülebilir Kalkınma Amaçları

• 3

• MakaleYalnız künye2016Scopus SJRQ2/r/bayburt/12391
  In 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.

  • 
  AtıfScopus49·WoS49·OpenAlex56

  İncele
• MakaleAçık Erişim2015Scopus SJRQ2/r/bayburt/13905
  The 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.

  • 
  AtıfScopus17·WoS16·OpenAlex19

  İncele
• MakaleAçık Erişim2013Scopus SJRQ2/r/bayburt/14154
  Carbonic 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.

  • 
  AtıfWoS27·OpenAlex32

  İncele