Abstract
An amperometric technique has been developed for the determination of enzyme activity by the detection of the decrease in the concentration of NADH used as the co-factor of the enzyme reaction. A glassy carbon electrode modified by adsorption of Mg++ and NADH is employed for the measurement of the anodic peak current corresponding to the oxidation of NADH.
Enzyme activity data of standard lactate dehydrogenase enzyme preparations obtained by the above amperometric technique were comparea with the results of a spectrophotometric method.
No significant deviation was found between the results obtained by the two different techniques.