Purification and characterization of the glycoprotein allergen from Prosopis juliflora pollen.
Highly active glycoprotein allergens have been isolated from pollen of Prosopis juliflora by a combination of Sephadex G-100 gel filtration and Sodium dodecyl sulphate-Poly-acrylamide gel electrophoresis. The glycoprotein fraction was homogeneous, and had molecular weight 20,000. The purified glycoprotein allergen contained 20% carbohydrate, mainly arabinose and galactose. Enzymatic digestion of glycoprotein with protease released glycopeptides of molecular weight ranging from less than 1,000 to more than 5,000 on Sephadex G-25 gel filtration. Antigenicity or allergenicity testing of these glycopeptides by immunodiffusion, immunoelectrophoresis, and radioallergosorbent test indicated complete loss of allergenic activity after digestion with protease whereas incubation with beta-D-galactosidase and periodate oxidation had little affect on the allergenic activity of the glycoprotein fraction. But incubation with alpha-D-glucosidase did not affect the allergenic activity significantly. All these tests indicated that protein played significant role in allergenicity of P. juliflora pollen.
Thakur
I S
IS
Department of Environmental Sciences, College of Basic Sciences and Humanities, G.B. Pant University of Agriculture and Technology, Pantnagar, Nainital, India.
D000485:Allergens / Q000302:isolation & purification*; D005591:Chemical Fractionation; D007887:Fabaceae / Q000276:immunology*; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D010946:Plants, Medicinal; D011058:Pollen / Q000276:immunology*
D000485:Allergens; D006023:Glycoproteins