Isolation and partial characterization of two antigenic glycoproteins from rye-grass (Lolium perenne) pollen.
Two glycoproteins have been purified from a buffer extract of rye-grass (Lolium perenne) pollen. Both migrated as single bands on sodium dodecyl sulphate/polyacrylamide gels. Glycoprotein 1 (0.8 mg/g of pollen) had a apparent mol.wt. of 33 000 and contained 95% protein and 5% carbohydrate. The monosaccharides glucose, galactose, mannose, arabinose and N-acetylglucosamine were present in the proportions 3:3:1:2:1. Glycoprotein 2 (0.4 mg/g of pollen) had an apparent mol. wt. of 68000 and contained 88% protein and 12% carbohydrate. The monosaccharides glucose, galactose, mannose, fucose, xylose, arabinose and N-acetylglucosamine were present in the proportions 4:7:13:5:8:6:6. This glycoprotein bound concanavalin A and Lotus tetragonolobus (asparagus pea) lectin. Radioallergosorbent (RAST) inhibition tests showed that Glycoprotein 1 is an effective allergen, whereas Glycoprotein 2 has less allergenic activity. A method for performing both lectin-binding assays and RAST inhibition tests using microtitre trays is described.
D000596:Amino Acids / Q000032:analysis; D000937:Antigen-Antibody Reactions; D002241:Carbohydrates / Q000032:analysis; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification*; D010940:Plant Proteins / Q000276:immunology / Q000302:isolation & purification*; D011058:Pollen / Q000276:immunology*; D012434:Secale
D000596:Amino Acids; D002241:Carbohydrates; D006023:Glycoproteins; D010940:Plant Proteins