Specific characters of serum MAO in dogs.

The effect of Tris-hydroxymethylaminomethane (Tris) on MAO activity in dog serum was studied by a modification of the method of McEwen and Cohen. Partially purified MAO from dog serum was inhibited 75% and 31% by 10 mM and 1 nM Tris, respecitively. The inhibitory effect of Tris was 1/10 of that by nialamide and 1/1000 of that by catron. Tris also slightly inhibited MAO activity in rabbit serum, but did not affect MAO from bovine or human serum, or from dog liver, kidney or brain. The extent of inhibition of dog serum MAO by Tris remained constant during incubation for 3 hrs. The inhibition was found to be reversible and noncompetitive. Benzylamine was most rapidly oxidized by MAO of dog serum followed in order by amylamine, beta- phenylethylamine and tyramine, while tryptamine and serotonin were not oxidized. Tris inhibited MAO activity with benzylamine or butylamine as substrates, but it was scarcely inhibitory with tyramine or beta-phenylethylamine as substrate. This work shows that Tris is a specific inhibitor of dog serum MAO and suggests that dog serum MAO may differ in enzymic properties from MAO in other animals.