Abstract
p-Sulfamoylbenzylamine and p-hydroxybenzylamine are shown to be substrates for monoamine oxidase A and for monoamine oxidases A and B, respectively. This was established by studies on the selectivity of benzylamine derivatives as substrates using monoamine oxidase inhibitors. A sensitive fluorimetric method for the separate assay of monoamine oxidases A and B is described. p-Sulfamoylbenzaldehyde and benzaldehyde formed enzymatically from p-sulfamoylbenzylamine and benzylamine, a known substrate for monoamine oxidase B, are quantified by means of the selective fluorimetric determination of aromatic aldehydes with 2,2′-dithiobis(1-aminonaphthalene). The limits of detection for the p-sulfamoylbenzaldehyde and benzaldehyde formed enzymatically are, respectively, 300 and 150 pmol per assay tube. Monoamine oxidases A and B in rat brain mitochondrial tissue and human platelets were assayed.
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