An arabinogalactan-protein (AGP) with a molecular mass of 110 kDa was isolated from whole grain of rye (Secale cereale L.) by double precipitation with (beta-D-Glc)3-Yariv-phenylglycoside (3GlcY) and its structure was analyzed. The AGP consists of a hydroxyproline-rich protein backbone of about 7 % and an arabinogalactan moiety of about 93%. By alkaline hydrolysis, hydroxyproline was identified as the main amino acid responsible for the binding between the protein and the carbohydrate subunits via an O-glycosidic linkage. The arabinogalactan moieties are highly branched consisting of 1,3-linked Galp residues, some of them linked in position 6 to 1,6-Galp side chains, terminating in Araf residues. With regard to its structure, the rye AGP is comparable to other cereal AGPs like those from oat or wheat grain.
