In this work three kinds of N-acetyl-D-glucosamine transferase were purified from the crude extract of pupae of Papilio, xuthus Linne through Sephadex G-25 gel filtration chromatography and CM-Sephadex C-50 ion exchange chromatography. Thermal stability of these enzymes were 35-55 degrees C and optimal pH for transferase activity appeared at 6.5-7.0. Each enzyme could react with N-acetyl-D-glucosamine, and produced insoluble deposit suggesting highly polymerized chitooligosaccharides. These catalytic properties somewhat differ from those of chitintransferase purified from pupae of Pieridae belonging to the same order.