Tissue origin of individual component proteins in crude extract of adult Paragonimus westermani was investigated. Major soluble component proteins were separated by disc-PAGE in 8% slab gel. By predefined Rf values, strips of gel containing each band protein was cut out. Each band protein was eluted by electrophoresis. Monospecific antibodies were prepared by immunizing rabbits with each band protein. When peroxidase-antiperoxidase (PAP) staining was done, antiserum to Band 1 reacted to content of eggs both in the worm and in the infected lung tissue. Antiserum to Band 2 reacted to parenchymal tissue of the worm. Antiserum to Band 4 showed the positive reaction at intestinal content while that to Band 5 reacted to the intestinal epithelial border. Antiserum to combined proteins of Bands 6/7 and that to Band 8 reacted to parenchymal tissue of the worm respectively. From the results, the origin of individual proteins in crude extract of adult P. westermani could be differentiated.
