Identification of twelve O-glycosylation sites in equine chorionic gonadotropin beta and equine luteinizing hormone ss by solid-phase Edman degradation

dc.contributor.authorBousfield, George R.en_US
dc.contributor.authorButnev, Vladimir Y.en_US
dc.contributor.authorButnev, Viktor Y.en_US
dc.date.accessioned2012-01-24T17:49:27Z
dc.date.available2012-01-24T17:49:27Z
dc.date.issued2001-01en_US
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractThe 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.en_US
dc.description.sponsorshipNIA NIH HHS/ NIDDK NIH HHSen_US
dc.description.versionpeer revieweden_US
dc.identifier11133668en_US
dc.identifierAG15428/ DK52383en_US
dc.identifier0207224en_US
dc.identifier.citationBiology of reproduction. 2001 Jan; 64(1): 136-47.en_US
dc.identifier.issn0006-3363en_US
dc.identifier.urihttp://dx.doi.org/10.1095/biolreprod64.1.136
dc.identifier.urihttp://hdl.handle.net/10057/4170
dc.language.isoengen_US
dc.publisherSociety for the Study of Reproductionen_US
dc.relation.ispartofseriesBiology of reproductionen_US
dc.rights.holderCopyright @ Society for The Study of Reproductionen_US
dc.sourceNLMen_US
dc.subjectComparative Studyen_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCarbohydrate Conformationen_US
dc.subject.meshCarbohydrates/analysisen_US
dc.subject.meshChorionic Gonadotropin/chemistryen_US
dc.subject.meshGlycopeptides/chemistryen_US
dc.subject.meshGlycoprotein Hormones, alpha Subunit/chemistryen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHorsesen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshHydrolysisen_US
dc.subject.meshLeydig Cells/drug effectsen_US
dc.subject.meshLuteinizing Hormone/chemistryen_US
dc.subject.meshMaleen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshProtein Multimerizationen_US
dc.subject.meshRadioligand Assayen_US
dc.subject.meshRatsen_US
dc.subject.meshReceptors, LH/metabolismen_US
dc.subject.meshTestosterone/biosynthesisen_US
dc.subject.meshChorionic Gonadotropin/metabolismen_US
dc.subject.meshChorionic Gonadotropin/pharmacologyen_US
dc.subject.meshGlycopeptides/metabolismen_US
dc.subject.meshGlycoprotein Hormones, alpha Subunit/metabolismen_US
dc.subject.meshLeydig Cells/metabolismen_US
dc.subject.meshLuteinizing Hormone/metabolismen_US
dc.subject.meshLuteinizing Hormone/pharmacologyen_US
dc.titleIdentification of twelve O-glycosylation sites in equine chorionic gonadotropin beta and equine luteinizing hormone ss by solid-phase Edman degradationen_US
dc.typeArticleen_US
Files