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dc.contributor.authorButnev, Viktor Y.en_US
dc.contributor.authorGotschall, R. Russellen_US
dc.contributor.authorBaker, Vanda L.en_US
dc.contributor.authorMoore, William T.en_US
dc.contributor.authorBousfield, George R.en_US
dc.date.accessioned2012-01-24T17:48:40Z
dc.date.available2012-01-24T17:48:40Z
dc.date.issued1996-06en_US
dc.identifier8641207en_US
dc.identifierHD-29047en_US
dc.identifier0375040en_US
dc.identifier.citationEndocrinology. 1996 Jun; 137(6): 2530-42.en_US
dc.identifier.issn0013-7227en_US
dc.identifier.urihttp://dx.doi.org/10.1210/en.137.6.2530
dc.identifier.urihttp://hdl.handle.net/10057/4142
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractThree equine CG (eCG) forms with identical amino acid sequences but different mol wt and monosaccharide compositions were isolated from a crude eCG preparation and designated eCG-L (low mol wt), eCG-M (medium mol wt), and eCG-H (high mol wt). No differences in primary structure between each form and the known sequence of eCG were observed. SDS-PAGE of these preparations under reducing conditions revealed that the mol wt differences between them were due only to the different sizes of their beta-subunits. Carbohydrate compositions suggested an increase in O-glycosylation in the higher mol wt forms. N-Linked glycopeptide fragments obtained from eCG beta-subunits by endoproteinase Lys-C digestion had identical electrophoretic mobilities. Thus, the different molecular sizes of the beta-subunits were associated only with disparities in O-glycosylation of their C-terminal extension. When tested in a LH and several FSH radioligand assay systems, eCG-H proved to have significantly lower receptor-binding activities than eCG-L and eCG-M. Endo-beta-galactosidase digestion increased the FSH receptor-binding activity of all eCG forms; however, partially deglycosylated eCG-H remained the least active form. Thus, the O-linked oligosaccharides of eCG-H exert a negative influence on its receptor-binding activity.en_US
dc.description.sponsorshipNICHD NIH HHSen_US
dc.language.isoengen_US
dc.publisherThe Endocrine Societyen_US
dc.relation.ispartofseriesEndocrinologyen_US
dc.sourceNLMen_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.meshChorionic Gonadotropin/chemistryen_US
dc.subject.meshChromatography, Gelen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshGlycopeptides/chemistryen_US
dc.subject.meshGlycoside Hydrolasesen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHorsesen_US
dc.subject.meshMaleen_US
dc.subject.meshMetalloendopeptidases/metabolismen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshMonosaccharides/analysisen_US
dc.subject.meshOligosaccharides/chemistryen_US
dc.subject.meshRatsen_US
dc.subject.meshReceptors, FSH/metabolismen_US
dc.subject.meshReceptors, LH/metabolismen_US
dc.subject.meshSheepen_US
dc.subject.meshStructure-Activity Relationshipen_US
dc.subject.meshbeta-Galactosidase/metabolismen_US
dc.subject.meshChorionic Gonadotropin/metabolismen_US
dc.subject.meshGlycopeptides/metabolismen_US
dc.titleNegative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin on its luteinizing hormone and follicle-stimulating hormone receptor-binding activitiesen_US
dc.typeArticleen_US
dc.description.versionpeer revieweden_US


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