Beta-subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different asparagine-linked oligosaccharide chains

Matsui, T.; Sugino, H.; Miura, M.; Bousfield, G.R.; Ward, D.N.; Titani, K.; Mizuochi, T.

Biochemical and Biophysical Research Communications 174(2): 940-945

1991


ISSN/ISBN: 0006-291X
PMID: 1704232
Accession: 007054574

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Abstract
The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a .beta.-subunit with an identical amino acid sequence. The Asn-linked oligosaccharide chains of eCG.beta. and eLH.beta. were quantitatively liberated as tritium-labeled oligosaccharides by hydrazinolysis followed by N-acetylation and NaB3H4-reduction. Paper electrophoresis in combination with sialidase digestion and solvolytic desulfation indicated that eCG.beta. contained neutral and sialylated oligosaccharides, while eLH.beta. contained neutral, sialylated, sulfated, and both sialylated and sulfated oligosaccharides. In addition, elution profiles on a Bio-Gel P-4 column of the neutralized oligosaccharide mixtures of eCG.beta. and eLH.beta. were different, indicating that the molecular masses of oligosaccharides of the two glycoproteins are different. Therefore, this suggests that the structures of the Asn-linked oligosaccharide chains of eCG.beta. and eLH.beta. are different although they have an identical amino acid sequence.