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1 January 2001 Identification of Twelve O-Glycosylation Sites in Equine Chorionic Gonadotropin β and Equine Luteinizing Hormone β by Solid-Phase Edman Degradation
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Abstract

The O-glycosylation sites for equine LHβ (eLHβ) and eCGβ were identified by solid-phase Edman degradation of four glycopeptides derived from the C-terminal region. Both subunits were O-glycosylated at the same 12 positions, rather than the 4–6 sites anticipated. These sites were partially glycosylated, with carbohydrate attachment ranging from 20% to 100% for eCGβ and from 10% to 100% for eLHβ. When the C-terminal peptide containing all but one of the O-linked oligosaccharides was removed by mild acid hydrolysis of either eLHβ or eCGβ, hybrid hormones could be obtained by reassociating eLHα,eFSHα, or eCGα with the truncated β subunit derivatives. These hybrid hormones were identical in LH receptor-binding activity when des(121-149)eLHβ or des(121-149)eCGβ were combined with the same α subunit preparation. Thus, O-glycosylation appears to be responsible for the β subunit contribution to the substantial difference in LH receptor-binding activity between eLH and eCG. Comparison of the equid LH/CGβ sequences with those available for the primate CGβ subunits indicated a greater conservation of glycosylation patterns in the former.

George R. Bousfield, Vladimir Y. Butnev, and Viktor Y. Butnev "Identification of Twelve O-Glycosylation Sites in Equine Chorionic Gonadotropin β and Equine Luteinizing Hormone β by Solid-Phase Edman Degradation," Biology of Reproduction 64(1), 136-147, (1 January 2001). https://doi.org/10.1095/biolreprod64.1.136
Received: 11 May 2000; Accepted: 15 August 2000; Published: 1 January 2001
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