Purification and characterization of the glycoprotein allergen from Prosopis juliflora pollen
Thakur, I.S.
Biochemistry International 23(3): 449-459
1991
ISSN/ISBN: 0158-5231 PMID: 1877983 Document Number: 376723
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 clycoprotein 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.