Description:
<jats:p><jats:bold>Abstract—</jats:bold> Comparative studies were carried out on 5‐hydroxytryptamine (5‐HT) and 3,4‐dimethoxyphenylethylamine (DMPEA) oxidation using brain homogenates from different animals as the source of enzyme. Differences in the enzyme saturation curves, in the inhibitor spectra and variations of enzyme activity depending on the substrate used, suggested that the enzymes taking part in the oxidation of 5‐HT and of DMPEA slightly differ from each other. Differences were interpreted on the basis of the heterogeneity of monoamine oxidase (MAO), suggested by earlier investigations. Thus the possibility of an individual inhibition of the degradation of certain amines has to be considered.</jats:p>