Identification of twelve O-glycosylation sites in equine chorionic gonadotropin beta and equine luteinizing hormone ss by solid-phase Edman degradation
| Autor: | G R, Bousfield, V Y, Butnev |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Male
Glycosylation Hydrolysis Molecular Sequence Data Carbohydrates Glycopeptides Leydig Cells Hydrogen-Ion Concentration Luteinizing Hormone Receptors LH Chorionic Gonadotropin Rats Radioligand Assay Glycoprotein Hormones alpha Subunit Carbohydrate Conformation Animals Testosterone Amino Acid Sequence Horses Protein Multimerization |
| Zdroj: | Biology of reproduction. 64(1) |
| ISSN: | 0006-3363 |
| Popis: | 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 eLHalpha,eFSHalpha, or eCGalpha 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 alpha 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|