Abstract
Monoamine oxidase (MAO) activity was determined in homogenates of larvae and pupae of the European corn borer, Ostrinia nubilalis (Hubner), and the tobacco bud worm, Heliothis virescens (F.), by using 214C-tryptamine as a substrate. Optimum activity was produced by addition of dithiotbreitol to the homogenizing medium and by removing the oxygen from this solution with nitrogen before homogenization. More than 80% of the activity was found in the supernatant fraction of the homogenate resulting from centrifugation at 105,000-g equivalents. Activity was inhibited by addition of s -triazines and by some known MAO inhibitors. Homogenates prepared at different times of day had different levels or activity.
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