Characterization of grass pollen allergens by affinity chromatography on Concanavalin A-Sepharose.
Glycoprotein allergens of different carbohydrate composition can be separated by lectin interaction in affinity chromatography. The present study shows that several differences exist in the sugar moiety both within the species and between different grass species. Experiments with Bermuda grass and common reed indicate that these 2 extracts possess allergens with a high affinity for Con A-Sepharose. This offers a simple and rapid method for isolation and purification of the major allergenic components of these 2 species in combination with more conventional separation techniques. The purity of single allergens may vary markedly depending on the occurrence of other interfering, non-allergenic substances having free terminal alpha-D-mannopyranoside or alpha-D-glycopyranoside residues which bind to the immobilized lectin.
D000485:Allergens / Q000032:analysis* / Q000302:isolation & purification; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008970:Molecular Weight; D006109:Poaceae / Q000276:immunology; D011058:Pollen / Q000276:immunology*; D011134:Polysaccharides / Q000494:pharmacology*; D011852:Radioallergosorbent Test; D012685:Sepharose / Q000031:analogs & derivatives / Q000494:pharmacology*
D000485:Allergens; D011134:Polysaccharides; C028326:concanavalin A-sepharose; D012685:Sepharose