title: Distribution of allergen activity and identification of the main IgE-binding glycopeptide of Parietaria judaica pollen.
abstract: Parietaria judaica pollen extract was separated by preparative isoelectric focusing and showed two allergenic components (A1 and A2) heterogeneously distributed within the pH gradient (pH 3-10). By fused-rocket immunoelectrophoresis, A1 was detected from pH 3 to 10, whereas A2 was only found at pH values below 8. Both components, A1 and A2, showed IgE-binding ability throughout their pH ranges, as determined by crossed-radio immunoelectrophoresis. In addition, all the preparative isoelectric focusing fractions contained the main allergenic polypeptide of P. judaica (Pj10) when analyzed by SDS-PAGE. This polypeptide was shown to be a glycopeptide or to be bound to a glycoprotein with alpha-D-mannopyranoside or alpha-D-glycopyranoside residues. Implication of charged sugar residues in the wide distribution of P. judaica allergens in a pH gradient is discussed.
mesh_terms: D000485:Allergens / Q000032:analysis*; D001666:Binding Sites, Antibody; D002623:Chemistry Techniques, Analytical; D003208:Concanavalin A / Q000276:immunology; D006020:Glycopeptides / Q000032:analysis*; D007073:Immunoglobulin E / Q000276:immunology*; D007525:Isoelectric Focusing; D010936:Plant Extracts / Q000276:immunology*
chemical_list: D000485:Allergens; D006020:Glycopeptides; D010936:Plant Extracts; D003208:Concanavalin A; D007073:Immunoglobulin E