Abstract
Triton X-114 has been employed to isolate integral membrane proteins from Schistosoma japonicum and Schistosoma mansoni adult worms. Suitable marker molecules and antisera directed or raised against schistosome proteins partitioned by Triton X-114 extraction indicated that the phase separation and purification of integral membrane proteins had been successful and this fraction was free of contamination with aqueous (soluble) or secretory antigens. Two dimensional immunoblots further exemplified differences between antigens in the integral membrane protein extract and those of the aqueous fraction. Seven S. japonicum integral membrane proteins have been identified on immunoblots by serum from a hyperimmune and an infected rabbit and by sera from Philippine patients with a history of schistosomiasis japonica. Integral membrane proteins of S. mansoni and S. japonicum had surprisingly little conformity in the molecular weights and electrophoretic mobilities between the two species.
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