title: Evidence for a single glycan moiety in rabbit serum transferrin and location of the glycan within the polypeptide chain.
abstract: The sequential removal of N-acetylneuraminic acid from rabbit serum transferrin has been followed by urea-polyacrylamide gel electrophoresis. The electrophoretic pattern is consistent with the presence of a single biantennary glycan chain. From the amino acid sequence of the carbohydrate-containing cyanogen bromide fragment we have shown that the glycan is attached to an asparaginyl side chain at a position equivalent to residue 491 in the sequence of human serum transferrin.
authors.affiliation: Division of Biochemistry, UMDS, Guy's Hospital, London, England.
authors.forename: R W
authors.initials: RW
authors.lastname: Evans
authors.forename: A
authors.initials: A
authors.lastname: Aitken
authors.forename: K J
authors.initials: KJ
authors.lastname: Patel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D003488:Cyanogen Bromide; D006023:Glycoproteins; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D011817:Rabbits; D014168:Transferrin / Q000302:isolation & purification
chemical_list: D002241:Carbohydrates; D006023:Glycoproteins; D010446:Peptide Fragments; D014168:Transferrin; D003488:Cyanogen Bromide