The serovar-specific main antigen (TM antigen) of Leptospira interrogans serovar canicola, which has lipopolysaccharide properties, was treated with 0.1 N sodium hydroxide. This treatment degraded the antigen into two major antigenic components, one of high and one of low molecular weight. The component with the lower molecular weight (approximately 4,000 daltons) consisted mainly of carbohydrates, having lost almost all of the fatty acid and protein components of the original antigen. Although the substance lacked immunoprecipitable activity, it continued to show serovar-specific inhibitory potency in a radioimmunoassay system as well as in a microscopic immunoagglutination reaction of the organisms. The antigenic activity of the compound was also reduced by periodate oxidation as was that of the TM antigen. A component with the same chemical and physicochemical properties was also produced by alkaline treatment from a different serotype TM antigen (serovar kremastos Kyoto), but it showed no antigenic activity. Leptospiral serovar-specific main (TM) antigen has been extracted from several organisms of different serovars. The TM antigen possesses chemical and physicochemical properties similar to those of the lipopolysaccharide antigens of gram-negative bacteria (1,2, 10, 15, 16). The antigenic activity of TM antigen is destroyed by periodate oxidation (10, 11). A carbohydrate portion demonstrating antigenic activity was isolated from the TM antigen of serovar kremastos Kyoto by formic acid hydrolysis (Y. Kawaoka, M. Naiki, and R. Yanagawa, in preparation) .In this study, TM antigen was treated with mild alkali to cleave the ester bonds, and it was found that this treatment also produced a carbohydrate fragment with antigenic activity.