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    Examination of Changes in Enzyme Activities of Erythrocyte Glucose 6-Phosphate Dehydrogenase and 6-Phosphogluconate Dehydrogenase in Rats Given Naringenin and Lead Acetate
    (2015) Demirdag, Ramazan; Comakli, Veysel; Ozkaya, Ahmet; Sahin, Zafer; Dag, Uzeyir; Yerlikaya, Emrah; Kuzu, Muslum
    In our study, controlled experimental groups were performed by giving substances Lead acetate, Naringenin andNaringenin+Lead acetate to rats in vivo conditions Changes in the glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) enzyme activities in erythrocytes of rats in these groups were compared to the Control group. An inhibition significant degree for G6PD enzyme activity was observed in all groups when compared to the Control group (p < 0.001). While inhibition significant degree for 6PGD enzyme activity was observed in Lead acetate groups (p < 0.001), no significant effect was observed in the Naringenin and Naringenin + Lead acetate groups (p > 0.05). In addition, lead levels in the groups of rats were determined using an inductively coupled plasma mass spectrometer (ICP-MS) device. As a result of measurements by the ICP-MS device, lead levels were found as an average of 42.9 ± 2.51, 36.71 ± 1.13, 172.16 ± 9.63, and 95.07 ± 5.87 ppm in the Control, Naringenin, Lead acetate and Naringenin+Lead acetate groups, respectively. Our results were shown thatNaringenin has protective effects on the Lead acetate induced oxidative stress erythrocytes in rat.
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    Öğe
    Inhibitory properties of some heavy metals on carbonic anhydrase I and II isozymes activities purified from Van Lake fish (Chalcalburnus Tarichi) gill
    (Springer, 2018) Kuzu, Muslum; Comakli, Veysel; Akkemik, Ebru; Ciftci, Mehmet; Kufrevioglu, Omer Irfan
    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 mu M for CA I isozyme and 6.16, 20.29, 46, and 223 mu M for CA II isozyme respectively.
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    Öğe
    Purification and Characterization of Carbonic Anhydrase from A. gri Balik Lake Trout Gill (Salmo trutta labrax) and Effects of Sulfonamides on Enzyme Activity
    (Wiley, 2015) Demirdag, Ramazan; Comakli, Veysal; Kuzu, Muslum; Yerlikaya, Emrah; Senturk, Murat
    Carbonic anhydrase (CA) was purified from Ar Balk Lake trout gill (fCA) by affinity chromatography on a sepharose 4B-tyrosine-sulfanilamide column. The fCA enzyme was purified with about a 303.9 purification factor, a specific activity 4130.4 EU (mg-protein)(-1), and a yield of 79.3 by using sepharose-4B-l tyrosine-sulfanilamide affinity gel chromatography. The molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was found to be about 29.9 kDa. The kinetic parameters, K-M and V-max were determined for the 4-nitrophenyl acetate hydrolysis reaction. Some sulfonamides were tested as inhibitors against the purified CA enzymes. The K-i constants for mafenide (1), p-toluenesulfonamide (2), 2-bromo-benzene sulfonamide (3), 4-chlorobenzene sulfonamide (4), 4-amino-6-chloro-1-3 benzenedisulfonamide (5), sulfamethazine (6), sulfaguanidine (7), sulfadiazine (8), and acetozazolamide (9) were in the range of 7.5-108.75 M. (C) 2014 Wiley Periodicals, Inc.
  • [ X ]
    Öğe
    Purification and Characterization of Carbonic Anhydrase from Agrı Balık Lake Trout Gill (Salmo trutta labrax) and Effects of Sulfonamides on Enzyme Activity
    (2015) Demirdag, Ramazan; Comakli, Veysel; Kuzu, Muslum; Yerlikaya, Emrah; Senturk, Murat
    Carbonic anhydrase (CA) was purified from Agrı Balık Lake trout gill (fCA) by affinity chromatography on a sepharose 4B-tyrosine-sulfanilamide column. The fCA enzyme was purified with about a 303.9 purification factor, a specific activity 4130.4 EU (mg-protein)–1, and a yield of 79.3 by using sepharose- 4B-L tyrosine-sulfanilamide affinity gel chromatography. The molecular weight determined by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) was found to be about 29.9 kDa. The kinetic parameters, KM and Vmax were determined for the 4-nitrophenyl acetate hydrolysis reaction. Some sulfonamides were tested as inhibitors against the purified CA enzymes. The Ki constants for mafenide (1), p-toluenesulfonamide (2), 2-bromo-benzene sulfonamide (3), 4-chlorobenzene sulfonamide (4), 4-amino-6- chloro-1–3 benzenedisulfonamide (5), sulfamethazine (6), sulfaguanidine (7), sulfadiazine (8), and acetozazolamide (9) were in the range of 7.5–108.75 µM.