The amylases of germinated triticale seeds were sequentially purified by ammonium sulfate precipitation, ion-exchange chromatography, and gel chromatography. Three different amylases were obtained in a pure state and tentatively designated as amylases I, II and III which each yielded a single band when examined by electrophoresis.   The respective specific activities of amylases I, II and III were 0.14-, 1.11- and 0.39-fold that of the crude enzyme extract.Amylases I, II and III had respective molecular weights of 62,000, 56,000 and 52,000. Amylase I showed the highest activity at pH 5.5 and 40℃ , amylase II at pH 5.0 and 50℃ , and amylase III at pH 5.0 and 40℃. Amylases I , II and III were stable in the range of pH 4.0-6.0 at below 50℃ . All activities of the enzymes were inhibited by mercury, PCMB, CH₂ICOOH, NI²⁺ and Cd²⁺ which may indicate that the SH group was necessary for activating the three enzymes. Each amylase specifically hydrolyzed starch and amylopectin, amylase III hydrolyzing lowmolecular- weight amylose particularly well. Amylase I hydrolyzed pullulan. A qualitative thinlayer chromatographic analysis of the products of this digestion revealed enzyme specificity. The decomposition products revealed amylase I to be α-amylase, and amylases II and III to be β-amylase.