Evidence for existence of A and B form monoamine oxidase in mitochondria from dog platelets.

It is known that platelet MAO appears to behave more like the B-form enzyme than the A-form enzyme based on inhibitor sensitivity and substrate specificity. However, dog platelets showed a different substrate specificity such as high activity with 5-HT and beta-PEA as substrates. Moreover, dog platelet MAO was sensitive to the drugs clorgyline and harmaline with 5-HT as the substrate, while it was sensitive to the drug deprenyl with beta-PEA as the substrate. These results also indicate the existence of two forms of MAO in dog platelets unlike in other platelets such as those from humans. A-form MAO from dog platelets was more stable against heat treatment at 55 degrees C than A-form MAO from dog liver and brain. On the other hand, there was no difference in the heat resistance of the three enzymes with beta-PEA as the substrate. After digestion with trypsin at 37 degrees C for 30 min, it was found that MAO from dog platelets, brain and liver were mostly inhibited with 5-HT as the substrate. In contrast, MAO in brain and liver were inhibited about 10%, but platelet MAO was inhibited about 50% with beta-PEA as the substrate. From these results, it is considered that dog platelet MAO exists as the two forms of the enzyme and has different enzymic properties in comparison with those of MAO from dog liver and brain mitochondria.