A new type of mitochondrial monoamine oxidase distinct from type-A and type-B

The characteristics of mitochondrial monoamine oxidase (MAO) in carp liver were studied with MAO inhibitors and substrates. This enzyme was thermolabile, but was stabilized in the presence of bovine serum albumin. With clorgyline and deprenyl, single-sigmoidal curves for inhibition of the activity towards tyramine or 5-hydroxytryptamine were obtained; the sensitivities to the two inhibitors were identical. The activity towards beta-phenylethylamine was not completely inhibited by clorgyline or deprenyl, but the remaining activity was inhibited by semicarbazide and the inhibition curves by either clorgyline or deprenyl and semicarbazide were also identical to the curves with the other two substrates. These results suggest that carp liver mitochondria contain "classical" MAO and a clorgyline- and deprenyl-resistant amine oxidase and that the classical MAO does not seem to be MAO-A or MAO-B, which are present in mitochondria of most mammalian tissues.