Isolation and Partial Characterization of Two Antigenic Glycoproteins from Rye-grass (Lolium Perenne) Pollen

Overview

Journal Biochem J

Specialty Biochemistry

Date 1981 Sep 1

PMID 7325979

Citations 10

Authors

B J Howlett

A E Clarke

Affiliations

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Abstract

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.

Citing Articles

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Purification and characterization of four beta-expansins (Zea m 1 isoforms) from maize pollen.

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N- and O-linked oligosaccharides of allergenic glycoproteins.

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Burge H, Rogers C Environ Health Perspect. 2000; 108 Suppl 4:653-9.

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Structural analysis of N-glycans from allergenic grass, ragweed and tree pollens: core alpha1,3-linked fucose and xylose present in all pollens examined.

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