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Protein P126, a parasitophorous vacuole major antigen of Plasmodium falciparum and precursor of 3 major exoantigens (50, 47, and 18 Kd in strain FCR-3) has been studied in 10 culture-adapted isolates originating from various endemic areas. Two monoclonal antibodies (specific for 50 and 47 Kd exoantigens, respectively) were used to immunoprecipitate culture supernatants and parasitized erythrocytes in each case. It was observed that all the parasite isolates reacted with both monoclonal antibodies, indicating the ubiquity of the epitopes analyzed. Further, two of the exoantigens (the 50 and 18 Kd of FCR-3) were found to have a stable molecular mass in all the isolates tested, whereas, the other one (47 Kd in FCR-3) was found to have a variable molecular mass, from 47 to 50 Kd. The molecular mass of the precursor varied from 126 Kd to 128 Kd. No correlation was found between geographic origin and antigenic size.