Wlhile studying the relation of the chemical composition of the living bark of the black locust tree (Robinia pseuidoacacia) to its frost resistance, 26,27) have observed marked seasonal fluctuations in the starch and sucrose contents of this tissue. The analytical data were suggestive of the existence of a temperature-sensitive starch-sucrose interconversion process, low temperature in late fall promoting a disappearance of starch and warm temiiperature of early spring promoting the production of starch with a proportionate and simiultaneous disappearance of sucrose. Because of the pronounced seasonal changes in the nature of the carbohydrate reserves in the black locust tree bark it was of interest to study enzyme systems which m-iight be involved. Further interest was attached to such a study because little information concerning the enzyme systems present in the living bark of trees is available. The presence of amylase and phosphorylase systems in the bark tissue of the black locust tree is established and characterization studies on these systems are presented here.The enzymilatic degradation of polysacchlarides of the starch-glycogen type miiay be hydrolytic, as catalyzed by amylases, or phosphorolytic, as catalyzed by phosphorylase. The mode of action of the amylases has been the subject of many studies and of several reviews (3,10,22,25). Two types of amnylase, a and ,8, are recognized. The a-amiiylases degrade starch preferentially by lhydrolyzing glycosidic linkages far removed from the terminal units. With prolonged incubations, however, a-amylase causes considerable conversion of starch to maltose together with the liberation of a small amount of glucose. /3-Amylase degrades starch by hydrolytic cleavage of successive imaltose units progressing from the non-reducing ends of the polysacelharide clhains. This action is stopped at the branching points of the amylopectin component of starch, but the degradation of the linear component approaches completion. The depolymerizing action of the amyl-1