An Arabinogalactan-protein from Rape Leaves

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A L-fucose-containing arabinogalactan-protein that strongly inhibited hemagglutination by eel anti-H agglutinin of human O erythrocytes was purified from hot phosphate-buffered saline extracts of mature leaves of rape, Brassica campestris. The purified glycoconjugate consisted of 90% of the polysaccharide moiety comprising L-fucose, L-arabinose, D-galactose, 4-O-methyl-D-glucuronic acid, and D-glucuronic acid, and 4% of the hydroxyproline-rich protein portion. Upon methylation, periodate oxidation, and enzymatic degradation, we found that consecutive β-(1→3)-linked D-galactopyranosyl residues constituted a backbone chain of the polysaccharide moiety, to which the side chains of β-(1→6)-linked D-galactopyranosyl residues were attached through O-6. Most of L-arabinofuranosyl residues were linked as single units through O-3 to the side chains while a small quantity of the sugar was present as (1→2)-, (1→3)-, or (1→5)-linked inter-chain residues. Single residues of α-L-fucopyranose, apparently attached to (1→2)-linked L-arabinofuranosyl residues, reacted with eel anti-H precipitin and Aleuria aurantia L-fucose-specific lectin, and were assumed to be crucial in the expression of the H-like activity. The uronosyl residues were also located at the non-reducing terminal ends. Reductive alkaline degradation of the arabinogalactanprotein provided indications that the polysaccharide chains were mainly conjugated through serine-O-glycosidic linkages to the polypeptide core. In an immunoprecipitation test, the rape leaf arabinogalactan-protein cross-reacted with antisera raised against radish leaf arabinogalactanprotein, indicating that these cruciferous arabinogalactan-proteins share common immunodeterminant(s) in their molecules.
社団法人日本農芸化学会の論文

An Arabinogalactan-protein from Rape Leaves

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