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 - 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.
AtıfScopus61WoS60OpenAlex64
İncele - MakaleYalnız künye2017Scopus SJRQ2Mechanism of capsaicin inhibition of aldose reductase activity
Alim, Zuhal; Kilinc, Namık; Sengul, Bulent; Beydemir, Sukru
Aldose reductase (AR) inhibitors play a vital importance as a potential therapeutic and preventive medicine when it comes to hyperglycemia associated diabetic complications. Additionally, capsaicin is used as a food additive and a drug in a number of diverse clinical trials. The aim of this study is to determine the in vitro inhibition behavior of capsaicin on AR enzyme activity, which was obtained from different rat tissues (heart, kidney, liver, and brain). We showed that AR was inhibited by capsaicin in the micromolar range and noncompetitive manner in all of the tissues. Ki values of capsaicin were found to be 8.87, 264, 535, and 597, respectively, in heart AR, kidney AR, liver AR, and brain AR. In conclusion, capsaicin may be an effective molecule when used in low concentrations to prevent diabetic complications associated with the polyol pathway.
AtıfScopus21WoS19OpenAlex24İncele