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    INHIBITORY EFFECTS OF SOME PESTICIDES AND METALS ON CARBONIC ANHYDRASE PURIFIED FROM SHABUT FISH (BARBUS GRYPUS) GILL TISSUE
    (Corvinus Univ Budapest, 2019) Yerlikaya, E.
    Carbonic anhydrase enzyme catalyzes the reversible inter-conversion of CO2 and HCO3. The enzyme is crucial for the osmotic balance and acid base regulation in the fish. It is well-known that gills of fish play the most important role in acid base relevant ion transfer, the transfer of H+ and/or HCO3, for the maintenance of systemic pH. Many researches have shown that fish are the species that is the most susceptible to environmental toxins. In addition, these toxins firstly encounter the gill tissue in fish. In this study, the carbonic anhydrase enzyme was purified 198.6-folds with 58.8% yield from Shabut Fish (Barbus grypus) gill tissue by Sepharose-4B-L-tyrosine-sulfanilamide affinity column. The specific activity was determined as 2.92 EU/mg protein. The molecular weight determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis was found to be about 29.9 kDa. Inhibitory effects of some pesticides (Spinosad and Dimethoate) and metal ions (Al3+, Cu2+, Ba2+, Fe2+, M2+, Se2+) were examined on the purified carbonic anhydrase enzyme. Inhibition graphics were drawn in order to find the IC50 values of metals and pesticides showing inhibition. The kinetic parameters of this enzyme were determined for its esterase activity, with 4-nitrophenyl acetate as substrate.
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    PURIFICATION, CHARACTERIZATION OF GLUTATHIONE S-TRANSFERASE FROM THE LIVER TISSUE OF GOOSE ( Anser anser Domesticus) AND INHIBITION EFFECTS OF SOME METAL IONS AND CHEMICALS
    (Pakistan Agricultural Scientists Forum, 2024) Sayin, Y.; Yerlikaya, E.; Demirdag, R.
    The GST enzyme is an antioxidant that protects organs against toxic substances. It reduces reactive oxygen species to less reactive metabolites. The GST enzyme has been studied in many living creatures such as sheep, birds, fish, bacteria, cattle, plants and humans. However, no studies on the Goose ( Anser anser Domesticus) liver GST enzyme (E.C. 2.5.1.18) have been found in the literature. This study demonstrates the purification and characterization of the GST enzyme from Goose ( Anser anser Domesticus) liver tissue by affinity chromatography. Besides, inhibitory effects of Hg2+, Ag2+and Fe2+cations and Oxytetracycline HCl, Tylosin Tartrate, Enrofloxacin and Doxycycline Hyclate chemicals on GST enzyme activity were investigated. The research was conducted under in vitro conditions using 1-Chloro-2,4dinitrobenzene method. The degree of purity of the enzyme solution was verified by SDS-PAGE. With the characterization of the enzyme, the optimal pH, optimal ionic strength and optimal temperature values were found to be 7.0, 100 mM and 40 degrees C, respectively. Separate inhibition graphs of Hg2+, Ag2+, Fe2+, Oxytetracycline HCl, Tylosin Tartrate, Enrofloxacin and Doxycycline Hyclate inhibitors were drawn. IC50 levels of inhibitors were found from the Activity%- [Inhibitor] graphs. As a result, the inhibition order of the inhibitors was found to be Hg2+ > Ag2+ > Fe2+ for cations, and Enrofloxacin < Tylosin Tartrate < Doxycycline Hyclate < Oxytetracycline HCl for chemicals.