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AI InsightGlutatyon S-transferaz enzimleri kemoterapik ilaçlar, çevresel karsinojenler, endojen moleküller olmak
📌 3 Maddede Bu Makale
Özet
Glutatyon S-transferaz enzimleri kemoterapik ilaçlar, çevresel karsinojenler, endojen moleküller olmak
Abstract
Glutathione S-transferase (GST) enzymes detoxify a broad spectrum of xenobiotics, including chemotherapeutic drugs, environmental carcinogens, and endogenous molecules. Glutathione transferases catalyze the conversion of some metabolites into less toxic substances. Phase II reactions, which often result in detoxification, are conjugation reactions of glutathione through GST enzymes that protect the organism from the attacks of highly reactive electrophilic substances. Since the GST enzyme can metabolize toxic exogenous compounds, it has been extensively investigated in mammals. In this study, the GST enzyme was purified in human erythrocytes with a specific activity of 5.56 EU mg-1 protein and a yield of 2316.0 fold with 65% efficienc. SDS-polyacrylamide gel electrophoresis was performed to check the purity of the purified enzyme and the molecular mass was determined to be about 26 kDa. The IC50 and Ki values for amoxycillin and vancomycin hydrochloride drugs on the purified GST enzyme were calculated and the type of inhibition was determined. As a result of the inhibition studies, we observed that these antibiotics inhibited the GST enzyme at low doses.