Side effects of aspirin on the structure and function of liver catalase

Catalase is an enzyme that catalyzes the breakdown of H2O2 into the oxygen and water molecules. On the other hand, aspirin is an important drug, which is used by many patients globally. Because of importance of catalase in antioxidant defense system and the connection between this enzyme and some diseases such as diabetes, in this study, we have investigated the effects of aspirin, which is metabolized in the liver like other drugs, on the structure and function of liver catalase. Using different spectroscopic (UV-Visible and Fluorescence) techniques at two temperatures of 25 and 37 0 C we have investigated the changes in the structure and function of catalase. By using kinetics studies obtained from spectroscopic methods as well as the Michaelis–Menten plot, the Km value was measured 40 mM. Kinetic results indicated that aspirin did not change the function of BLC. However, addition of aspirin caused a gradual reduction in the fluorescence emission intensity of catalase. Also‚ the values of binding constants of drug on the enzyme decreased by increasing the temperature. The results of the fluorescence studies showed a decrease in fluorescence emission spectra of catalase, affected by addition of aspirin. Aspirin acts as a quencher with unfolding the three- dimensional structure of catalase, but this unfolding did not inhibit the catalase activity