The activity change of mulberry seeds protease was compared during germination for 5 days at 28$^{circ}C$ in the dark place after daily hormone injection of different concentration. The protease from germinated mulberry seeds for 4 days was partially purified and the enzyme characteristics was investigated. The protease activity of mulberry seeds treated by hormone was highest with 10 $mu$m GA3 followed by 10 $mu$M zeatin and 10 $mu$M kinetin. The protease activity of mulberry seeds was increased by 14% with 10ml agar culture that control at 4th day of germination. The protease from mulberry seeds was purified 313 fold by DEAE-Toyo-pearl 650M, Butyl-Toyopearl, Hydrozylapatite and Toyopearl HW 55M. After purification, the specific activity of the enzyme was 175 units/mg. Optimum pH and temperature of protease from mulberry seeds was 5.0 and 37$^{circ}C$, respectively. The protease was stable below 37$^{circ}C$ and the enzyme activity was decreased by 50%, when incubated at 52$^{circ}C$ for 10minutes. The protease activity of mulberry seeds was inhibited by metal ions such as mercury, iron, zinc, copper, but activited by magnesium, choromium, aluminium ions. The Km value of the protease was 0.89mM with azocasein as a subscribe.