| Abstract: | The gluconic fragment of strophantin K oxidation by sodium metaperiodate yields a dialdehyde derivate conjugated with catalase. The conjugate obtained contains 11 molecules of cardiac glucoside. Adsorption and circular dichroism spectra of the native enzyme and its conjugate were compared and structural differences between both samples were revealed. The kinetics of ethanol oxidation into acetaldehyde by cumene hydroperoxide was studied at 30 degrees C in the phosphate buffer pH 6.6; this reaction was shown to proceed with the participation of catalase and its cat-str conjugate. The catalytic constants for catalase are 1.2-1.5 times as high as those for cat-str, whereas the Km values for both substrates for the conjugate as 1.5-2 times as high as those for catalase. Catalase modification by strophantin K increases the enzyme thermostability up to the isokinetic point of 40 degrees C; above this threshold the cat-str thermostability decreases as compared with the native enzyme. The thermodynamical activation parameters for catalase and cat-str inactivation were determined. |
