Abstract
The activity of bovine plasma amine oxidase is described by using high-performance liquid chromatography. As little as 2.0 pmol of 3, 4-dihydroxybenzaldehyde formed in the amine oxidase-catalyzed reaction could be detected using 3, 4-dihydroxybenzylamine as a substrate and 2.5 pmol of benzaldehyde for benzylamine. The above process was applied to the kinetic analysis of the inhibition reaction of the enzyme by procaine and procainamide. The Michaelis constants (Km) of the reaction were 5.3×10-4 M and 4.5×10-4 M for 3, 4-dihydroxybenzylamine and benzylamine respectively. The inhibition constants (Ki) of procaine and procainamide were 5.0×10-4 M and 88×10-4 M for 3, 4-dihydroxybenzylamine and 1.3×10-4 M and 5.3×10-4 M for benzylamine respectively.
