The 150 kDa protein of cyst fluid (CF) of Taenia solium metacestodes was purified by ammonium sulfate fractionation and Superose 6 HR gel filtration chromatography. The purified protein consisted of three subunits (15, 10 and 7 kDa proteins), which were analyzed with the use of a 7.5-15% gradient sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Immunofluorescence study was carried out by using immunize specific polyclonal antibody. Positive reactions were noticed at bladder walls, calcareous corpuscles, granules of cyst fluid and some host tissue surrounding the bladder wall of the metacestodes. These results suggest that the 150 kDa protein was secreted into host tissues, inducing immune responses in the host, and it may play important roles in the cellular physiology of the parasites.
Animals ; Chemical Fractionation ; Chromatography, Gel ; Cyst Fluid/*chemistry/metabolism/parasitology ; Cysticercosis/*metabolism/parasitology ; Electrophoresis, Polyacrylamide Gel ; Helminth Proteins/chemistry/*isolation & purification ; Mice ; Mice, Inbred BALB C ; Microscopy, Fluorescence ; Molecular Weight ; Support, Non-U.S. Gov't ; Swine ; Swine Diseases/parasitology ; Taenia solium/*metabolism