Structure of the tryptic glycopeptide isolated from rabbit transferrin

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Abstract
The structure of the tryptic glycopeptide isolated from rabbit transferrin was elucidated by use of sequential Edman degradations, specific exoglycosidases, endo-.beta.-N-acetylglucosaminidases, methylation analyses and periodate oxidation studies. The glycopeptide consists of a heteropolysaccharide, AcNeu.alpha.2 .fwdarw. 6Gal.beta.1 .fwdarw. 4GlcNAc.beta.1 .fwdarw. 2Man.alpha.1 .fwdarw. 3[AcNeu.alpha.2 .fwdarw. 6Gal.beta.1 .fwdarw. 4GlcNAc.beta.1 .fwdarw. 2Man.alpha.1 .fwdarw. 6]-Man.beta.1 .fwdarw. 4GlcNAc, attached to a peptide, Asn-Ser-Ser-Leu-Cys, via a linkage involving N-acetyl-glucosamine and asparagine. The stoichiometry of this glycopeptide is 2 mol/mol of protein; rabbit transferrin apparently contains 2 structurally identical glycopeptide segments.