The cellulase from internal organs of edible snails was purified by fractionation with ammonium sulfate, DEAE-Sephadex chromatography and gel filtration on Sephacryl S-200 and Superose 12 HR 10/30. The specific activity of the purified cellulase was 85.1 units/mg protein with 24.3 purification fold from crude extract. Molecular weight of the enzyme was estimated to be approximately 74,000 dalton by gel filtration chromatography and SDS-PAGE eletrophoresis. T7e isoelectric point of the enzyme was determined to be pH 4.6. The optimum temperature and pH of the enzyme were 5$0^{circ}C$ and pH 6.0, respectively. The enzyme was stable at 30~5$0^{circ}C$ and pH 6.0~10.0. It was activates by Mn$^{2+}$, but inhibited by Li$^{2+}$, Zn$^{2+}$, Ag$^{2+}$ and Hg$^{2+}$./TEX> 2+/.