TY - JOUR
T1 - β-Subunits of equine chorionic gonadotropin and lutenizing hormone with an identical amino acid sequence have different asparagine-linked oligosaccharide chains
AU - Matsui, Taei
AU - Sugino, Hiromu
AU - Miura, Mari
AU - Bousfield, George R.
AU - Ward, Darrell N.
AU - Titani, Koiti
AU - Mizuochi, Tsuguo
N1 - Funding Information:
‘This work was supported Research from the Ministry from Fujita Health University.
Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1991/1/31
Y1 - 1991/1/31
N2 - The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a β-subunit with an identical amino acid sequence. The Asn-linked oligosaccharide chains of eCGβ and eLHβ 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 eCGβ contained neutral and sialylated oligosaccharides, while eLHβ 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 eCGβ and eLHβ 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 eCGβ and eLHβ are different although they have an identical amino acid sequence.
AB - The glycoprotein hormones, equine chorionic gonadotropin (eCG) and lutenizing hormone (eLH), possess a β-subunit with an identical amino acid sequence. The Asn-linked oligosaccharide chains of eCGβ and eLHβ 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 eCGβ contained neutral and sialylated oligosaccharides, while eLHβ 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 eCGβ and eLHβ 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 eCGβ and eLHβ are different although they have an identical amino acid sequence.
UR - http://www.scopus.com/inward/record.url?scp=0026063708&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026063708&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(91)91509-B
DO - 10.1016/0006-291X(91)91509-B
M3 - Article
C2 - 1704232
AN - SCOPUS:0026063708
VL - 174
SP - 940
EP - 945
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -