Structure determination of the major N- and O-linked carbohydrate chains of the beta subunit from equine chorionic gonadotropin

Eur J Biochem. 1990 Apr 20;189(1):175-83. doi: 10.1111/j.1432-1033.1990.tb15474.x.


The carbohydrate moieties of equine chorionic gonadotropin alpha and beta subunits were released from the protein backbones by successive treatments with peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase F and alkaline borohydride and then fractionated by FPLC and HPLC. The major N- and O-linked glycans of the beta subunit were characterized by 500-MHz 1H-NMR spectroscopy, showing a remarkable structural heterogeneity for the N-glycosidically linked chains, comprising mono-, di-, tri- and tri'-antennary N-acetyllactosamine type of glycans, being partly alpha 1-6 fucosylated at the Asn-bound GlcNAc residue and having alpha 2-6 and alpha 2-3 linked N-acetyl- and N-acetyl-4-O-acetylneuraminic acid residues as sialic acid constituents. Significant differences in this respect were detected for the partially characterized glycans of the alpha subunit. The major part of the O-linked carbohydrate chains, occurring solely in the beta subunit, is formed by tri-, tetra-, penta- and hexa-saccharides. There are indications for the presence of oligo(N-acetyllactosamine) units in both the N- and O-linked glycans of the beta subunit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Carbohydrates / analysis
  • Chromatography, Gel
  • Gonadotropins, Equine* / isolation & purification
  • Horses
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Oligosaccharides / isolation & purification*
  • Peptide Fragments / isolation & purification


  • Carbohydrates
  • Gonadotropins, Equine
  • Oligosaccharides
  • Peptide Fragments