Abstract
An amperometric technique was developed for the determination of enzyme activity by detection of the decrease in concentration of the NADH used as co-factor for the enzyme reaction. A glassy carbon electrode modified by adsorption of Mg2+ and NADH is used for measurement of the anodic peak current corresponding to the oxidation of NADH. Enzyme activity data for standard lactate dehydrogenase [human EC 1.1.1.27] enzyme preparations obtained by this amperometric technique were compared with the results of a spectrophotometric method. No significant deviation was found between the results obtained by the 2 different techniques.