Ginseng proteins have been extracted and partially purified by the methods of ammonium sulfate fractionation, heat inactivation and Sephadex G-75 column chromatography. The final three fractions obtained (GI, GII and GIII) were subjected to paper chromatography and SDS-polyacrylamide gel electrophoresis. Molecular weights of polypeptide chains from each fraction were est-mated by the standard line obtained from the plot of electrophoretic mobilities against the logarithm of molecular weights of standard proteins. Results are as follows: 1) GI showed three protein spots and four polypeptides of which M.W. were 63,000, 60,000, 56,000, 51,000 and 34,200. 2) GII showed four protein spots and five polypeptides with their M.W. of 64,600, 56,000, 45,400, 35,800, end 25,200, 3) GIII showed three protein spots and four polypeptides with their M.W. of 66,000, 63,000, 56,000 and 22,000.