Characterization and isolation of concanavalin A binding sites from the epidermis of S. mansoni.
Using concanavalin A labeled with tritium and fluorescein isothiocyanate we studied the binding properties of this plant lectin to adult paired schistosomes. Using concanavalin A coupled to a sepharose column we attempted to isolate and characterize concanavalin A binding molecules from the epidermis of adult schistosomes. Our results indicate the presence of specific concanavalin A binding sites on the surface of adult Schistosoma mansoni. A significant percentage of the concanavalin A was specifically bound and showed characteristics similar to that identical in other concanavalin A binding tissues. The parasite's concanavalin A binding sites appear to be 2 or 3 high molecular weight glycoproteins. There is some indication that glycoproteins associated with the worm's epidermis function as enzyme(s). The immunological significance of these glycoproteins has not been determined.
D000818:Animals; D002122:Calcium Chloride / Q000494:pharmacology; D003208:Concanavalin A / Q000037:antagonists & inhibitors / Q000378:metabolism; D006023:Glycoproteins / Q000302:isolation & purification; D008297:Male; D008766:Methylmannosides / Q000494:pharmacology; D051379:Mice; D008970:Molecular Weight; D011952:Receptors, Concanavalin A / Q000302:isolation & purification*; D011955:Receptors, Drug / Q000302:isolation & purification*; D012503:Saponins / Q000494:pharmacology; D012550:Schistosoma mansoni / Q000378:metabolism*; D012867:Skin / Q000187:drug effects / Q000378:metabolism
D006023:Glycoproteins; D008766:Methylmannosides; D011952:Receptors, Concanavalin A; D011955:Receptors, Drug; D012503:Saponins; D003208:Concanavalin A; D002122:Calcium Chloride