Enzyme properties of monoamine oxidase in the frontal cortex and liver of the gerbil (Meriones unguiculatus).

Abstract 1. 1. Enzyme properties of monoamine oxidase (MAO) in the frontal cortex and liver of the gerbil were investigated using 5-hydroxytryptamine (5-HT), benzylamine (Bz) and tyramine (Tyr) as substrates. 2. 2. The K m values of MAO towards the three substrates were almost similar to the values in other species. The V max value of MAO towards Bz was much lower than the value towards 5-HT. 3. 3. In the inhibition studies with selective MAO-A and MAO-B inhibitors, clorgyline and deprenyl, deamination of 5-HT, Bz and Tyr in both tissues was induced by MAO-A alone, MAO-B alone and both forms of the enzyme, respectively, indicating the same substrate specificity as that in rats. 4. 4. The apparent proportion of MAO-A to MAO-B activities in the gerbil liver was approximately 6:4, whereas MAO-A in the frontal cortex of the gerbil was exclusively predominant, consistent with the previous data in the golden hamster which belongs to the same family as the gerbil.