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Regular Article |
a Department of Biological Sciences, Wichita State University, Wichita, Kansas 67260-0026
ABSTRACT
The O-glycosylation sites for equine LHß (eLHß) and eCGß 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 eCGß and from 10% to 100% for eLHß. When the C-terminal peptide containing all but one of the O-linked oligosaccharides was removed by mild acid hydrolysis of either eLHß or eCGß, hybrid hormones could be obtained by reassociating eLH
,eFSH, or eCG with the truncated ß subunit derivatives. These hybrid hormones were identical in LH receptor-binding activity when des(121-149)eLHß or des(121-149)eCGß were combined with the same subunit preparation. Thus, O-glycosylation appears to be responsible for the ß subunit contribution to the substantial difference in LH receptor-binding activity between eLH and eCG. Comparison of the equid LH/CGß sequences with those available for the primate CGß subunits indicated a greater conservation of glycosylation patterns in the former.
1 This work was supported by NIH grants AG15428 and DK52383.
2 Correspondence: George R. Bousfield, Department of Biological Sciences, Box 26, Wichita State University, 1845 Fairmount, Wichita, KS 67260-0026. FAX: 316 978 3772; bousfiel{at}twsuvm.uc.twsu.edu
3 Current address: Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, IA 52242.
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