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Bovine transferrin glycopeptide: the relevance of its structure to interaction with the mammalian hepatic lectin that binds asialoglycoproteins.

After proteolytic digestion of bovine transferrin (phenotype AA), a glycopeptide fraction was isolated by gel filtration and high-voltage electrophoresis. Two glycopeptide bands were recovered, each of which contained one residue of aspartic acid, two of serine, two of galactose, three of mannose, and four of N-acetyl glucosamine together with some fucose. However, the bands differed with respect to sialic acid content (two and three residues respectively). Using the same isolation procedures, a commercial sample of human transferrin yielded four glycopeptide bands (two major, two minor) on high-voltage electrophoresis. On analysis, the two major bands differed in amino-acid residues but their carbohydrate compositions were very similar. The analyses largely resembled previously published analytical data for two human transferrin glycopeptides (Jamieson, G. A., Jett, M. D Spik, G., Bayard, B., Fournet, B., Strecker. G., Bouquelet, S. &Montreuil, J. (1...