Structure of the tryptic glycopeptide isolated from rabbit transferrin.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D006020:Glycopeptides / Q000302:isolation & purification; D006026:Glycoside Hydrolases; D008968:Molecular Conformation; D010446:Peptide Fragments; D011817:Rabbits; D014168:Transferrin; D014357:Trypsin
D000596:Amino Acids; D002241:Carbohydrates; D006020:Glycopeptides; D010446:Peptide Fragments; D014168:Transferrin; D006026:Glycoside Hydrolases; D014357:Trypsin