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Abstract
A rapid and convinient method to study the kinetic and inhibition properties of rat brain monoamine oxidase form A by high-performance liquid chromatography is described. The procedure consists of homogenization of the brain tissue, enzymatic reaction with or without inhibitors using 5-hydroxytryptamine as the substrate, termination of the reaction with perchloric acid, removal of protein by centrifugation and detection of reaction products at 280 nm after HPLC separation. The method was applied to determine Km and Vmax values of 5-HT for MAO-A and to study the inhibition properties of MAO-A using clorgyline and 1-deprenyl as inhibitors.