The amount of citrate was determined by means of the Natelson method[11 (link)].
SOD activity was determined by the nitroblue tetrazolium recovery rate inhibition in the non-enzymatic system of phenazine methosulfate (PMS) and NADH.
The incubation medium, with a total volume of 3 mL, contained 0.1 M phosphate buffer (pH 7.8), 0.33 mmol/L EDTA, 0.41 mmol/L NBT, 0.01 mmol/L PMS, and 0.8 mmol/L NADH. The activity was measured spectrophotometrically according to the extinction augmentation after 5 min using the Hitachi U-1900 spectrophotometer at 540 nm[12 ].
Catalase activity was determined at a wavelength of 410 nm using the method based on the ability of hydrogen peroxide to form stable colored complex with ammonium molybdate[13 (link)].
The amount of the enzyme that was required for the conversion of 1 mM of substrate per min at 25 °C was defined as the enzyme unit (E). Biuret method was used to determine the protein content.