抄録
Glycoconjugates reacting with eel anti-H agglutinin were purified from extracts of leaves of three species of cruciferous plants (radish, turnip, and rape) by precipitation with ethanol, ionexchange chromatography, and gel filtration. High voltage paper electrophoresis or ultracentrifugal analysis revealed that the purified specimens were homogeneous.Their apparent molecular weights were estimated to range from 0.5 to 1.5×105. They consisted of a novel L-fucose-containing acidic arabinogalactan-protein composed of residues of L-arabinose, D-galactose, L-fucose, 4-O-methyl-Dglucuronic acid, and D-glucuronic acid in similar molar proportions, and containing polypeptide portions with abundant hydroxyproline, serine, threonine, and alanine. All the arabinogalactanproteins exhibited potent inhibitory activity against the hemagglutination of human O erythrocytes by eel anti-H agglutinin.
