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dc.contributor.authorGotschall, R. Russellen_US
dc.contributor.authorBousfield, George R.en_US
dc.date.accessioned2012-01-24T17:48:34Z
dc.date.available2012-01-24T17:48:34Z
dc.date.issued1996-06en_US
dc.identifier8641208en_US
dc.identifierHD-29047en_US
dc.identifier0375040en_US
dc.identifier.citationEndocrinology. 1996 Jun; 137(6): 2543-57.en_US
dc.identifier.issn0013-7227en_US
dc.identifier.urihttp://dx.doi.org/10.1210/en.137.6.2543
dc.identifier.urihttp://hdl.handle.net/10057/4131
dc.descriptionClick on the DOI link below to access the article (may not be free).en_US
dc.description.abstractEquine gonadotropin alpha-subunit glycosylation was examined by releasing oligosaccharides using a sequential enzymatic deglycosylation protocol and comparing the released oligosaccharide populations using a high resolution oligosaccharide mapping technique. Digestion of native alpha-subunit preparations with peptide-N-glycosidase altered their mobilities during SDS-PAGE under reducing conditions to positions intermediate between the corresponding native alpha-subunit and completely deglycosylated alpha-subunit bands. Complete alpha-subunit deglycosylation required reduction of disulfide bonds. Results of solid-phase Edman degradation demonstrated that partial deglycosylation occurred exclusively at Asn56. Oligosaccharide mapping of total oligosaccharides obtained by enzymatic deglycosylation of reduced, carboxymethylated alpha-subunit preparations revealed hormone-specific patterns of glycosylation in eLH alpha and eCG alpha. Oligosaccharide mapping of individual glycosylation sites revealed that hormone-specific glycosylation was primarily restricted to Asn56 of both subunit preparations and revealed a hormone-specific pattern of Asn56 glycosylation in eFSH alpha that was obscured in the total oligosaccharide map. eLH alpha Asn56 oligosaccharides appeared to be primarily seven variants of a monoantennary structure. eCG alpha Asn56 oligosaccharides consisted of one of two forms, either a sialylated biantennary oligosaccharide that appeared identical to a commercial carbohydrate standard or a lactosamine variant of that structure.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.meshAmidohydrolases/metabolismen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAsparagine/chemistryen_US
dc.subject.meshCyanogen Bromideen_US
dc.subject.meshDisulfides/chemistryen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshGlycoprotein Hormones, alpha Subunit/metabolismen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHorsesen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshOligosaccharides/metabolismen_US
dc.subject.meshPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidaseen_US
dc.subject.meshGlycoprotein Hormones, alpha Subunit/chemistryen_US
dc.subject.meshOligosaccharides/chemistryen_US
dc.titleOligosaccharide mapping reveals hormone-specific glycosylation patterns on equine gonadotropin alpha-subunit Asn56en_US
dc.typeArticleen_US
dc.description.versionpeer revieweden_US


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