Peroxidase activity and localization in the abscission zone of bean leaves were studied histochemically and by gel electrophoresis. Deblading of bean leaves resulted in an increase in peroxidase activity in the abseission zone 2 to 4 days after deblading with highest activity just prior to separation. In debladed plants, the Peroxidase has been implicated in a number of diverse phenomena observed in plants (29,31,34,35) including the synthesis of ethylene (21,38). Similarly, conflicting reports (10,18) indicate that ethylene synthesis is not regulated by peroxidase. The localized increase in protein and RNA synthesis necessary for separation to occur in the abscission zone of Phaseolus vulgaris is increased by ethylene (2) and has been associated with an increase in cellulase activity (1,15,26).The effect of ethylene on plant enzyme systems such as peroxidase has been well documented (11,12,16,31) (Figs. 1-4) was studied until separation was complete. Reagents for the localization of peroxidase (8,29) were: 1% H202 and a 70% ethanol solution of 0.1 M benzidine. The peroxidase reaction was carried out on a glass slide. A drop of each reagent was placed in contact with the fresh tissue slice. The sections were incubated for 1 to 2 min, the resulting bubbles were removed by rinsing twice with distilled water, and color photographs were taken immediately to record enzyme localization. Potassium cyanide (0