Characterization of glycopeptides derived from the low-density lipoprotein of hen's egg yolk

1 August 1968

journal article
Published by Canadian Science Publishing in Canadian Journal of Biochemistry

Vol. 46 (8) , 983-988
https://doi.org/10.1139/o68-147

Abstract

Two glycopeptides (A and B) were isolated from pronase-digested vitellenin, the protein moiety of the low-density lipoprotein of hen's egg yolk. Aspartic acid was the only N-terminal amino acid of both glycopeptides but only A contained N-acetylneuraminic acid. A contained 55% hexose (mannose), 14% hexosamine, 12% N-acetylneuraminic acid, 0.71% amide nitrogen, and its molecular weight was 2.3 × 10³. The corresponding values for B were 64, 17, 0.0, 0.75, and 2.0 × 10³. Chemical analyses showed that B (and probably A) occurs in vitellenin with the heteropolysaccharide group bound N-glycosidically via the β-amide group of an asparaginyl residue. The indicated structure is R∙(NH)Asp∙Thr∙Ser∙(Ala, Gly, Val)∙Ile, where R, the heteropolysaccharide group, contains 2 hexosamine and 8 hexose residues.

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