Structure of the tryptic glycopeptide isolated from rabbit transferrin.

Strickland DK, Hamilton JW, Hudson BG
Biochemistry. 1979 18 (12): 2549-54

PMID: 444474 · DOI:10.1021/bi00579a018

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, AcNeualpha2 leads to 6Galbeta1 leads to 4GlcNAcbeta1 leads to 2Manalpha1 leads to 3[AcNeualpha2 leads to 6Galbeta1 leads to 4GlcNAcbeta1 leads to 2Manalpha1 leads to 6]-Manbeta1 leads to 4GlcNAcbeta1 leads to 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, indicating that rabbit transferrin contains two structurally identical glycopeptide segments.

MeSH Terms (10)

Amino Acids Animals Carbohydrates Glycopeptides Glycoside Hydrolases Molecular Conformation Peptide Fragments Rabbits Transferrin Trypsin

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