Biochemical studies on the 30-40 kDa Schistosoma mansoni surface antigens.

Biochemical studies of the previously identified 30-40 kDa surface antigens of Schistosoma mansoni schistosomula confirmed that four molecules could be discriminated in this antigenic group. The antigens presented slightly different molecular mass in sodium dodecyl sulfate polyacrylamide gel electrophoresis (40, 38, 37 and 32 kDa) but were all found in isoelectric focusing at the same pH (6.2-6 and 7.5). The four antigens bound to concanavalin A and only the 32 kDa molecule had affinity for the Lens culinaris agglutinin. These results indicated almost similar biochemical characteristics of the 30-40 kDa antigens and partial hydrolysis of the 38 and 32 kDa antigens suggested that they were affected by a similar cleavage process. The possibility of a structural homology between these two components is discussed.