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dc.contributor.authorWalton, Wendy J.en_US
dc.contributor.authorNguyen, Van T.en_US
dc.contributor.authorButnev, Vladimir Y.en_US
dc.contributor.authorSingh, Vinoden_US
dc.contributor.authorMoore, William T.en_US
dc.contributor.authorBousfield, George R.en_US
dc.identifierAG15428/ CA-16520/ DK-19525en_US
dc.identifier.citationThe Journal of clinical endocrinology and metabolism. 2001 Aug; 86(8): 3675-85.en_US
dc.descriptionClick on the link below to access the article (may not be free).en_US
dc.description.abstractHuman FSH consists of a mixture of isoforms that can be separated on the basis of differences in negative charge conferred by variations in the numbers of sialic acid residues that terminate oligosaccharide branches. Western analysis of human FSH isoforms separated by chromatofocusing revealed the presence of two human FSHbeta isoforms that differed in size. A low mol wt human FSHbeta isoform was associated with all FSH isoform fractions. A high mol wt human FSHbeta isoform was associated with the more acidic fractions and increased in relative abundance as the pI decreased. Characterization of representative human FSHbeta isoforms by mass spectrometry and automated Edman degradation revealed a low mol wt isoform that was not glycosylated. A high mol wt isoform was N-glycosylated at Asn residues 7 and 24. These results indicate that pituitary human FSH consists of two classes of molecules: those that possess a nonglycosylated beta-subunit and those that possess a glycosylated beta-subunit. Glycoprotein hormones are known to be elliptical molecules, and the beta-subunit oligosaccharides project outward from the short diameter, thereby increasing it. It is interesting to speculate that this change in shape might affect ultrafiltration rates, leading to differences in delivery rates to target tissues and elimination by filtration in the kidney.en_US
dc.description.sponsorshipNIA NIH HHS/ NCI NIH HHS/ NIDDK NIH HHSen_US
dc.publisherThe Endocrine Societyen_US
dc.relation.ispartofseriesThe Journal of clinical endocrinology and metabolismen_US
dc.subjectResearch Support, U.S. Gov't, P.H.S.en_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshChorionic Gonadotropin/metabolismen_US
dc.subject.meshChromatography, Affinityen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFollicle Stimulating Hormone/chemistryen_US
dc.subject.meshFollicle Stimulating Hormone, beta Subunit/metabolismen_US
dc.subject.meshGranulosa Cells/drug effectsen_US
dc.subject.meshImmunoradiometric Assayen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshProtein Isoforms/chemistryen_US
dc.subject.meshRadioligand Assayen_US
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen_US
dc.subject.meshFollicle Stimulating Hormone/isolation & purificationen_US
dc.subject.meshFollicle Stimulating Hormone/pharmacologyen_US
dc.subject.meshFollicle Stimulating Hormone, beta Subuniten_US
dc.subject.meshGranulosa Cells/physiologyen_US
dc.subject.meshProtein Isoforms/isolation & purificationen_US
dc.subject.meshProtein Isoforms/pharmacologyen_US
dc.titleCharacterization of human FSH isoforms reveals a nonglycosylated beta-subunit in addition to the conventional glycosylated beta-subuniten_US
dc.description.versionpeer revieweden_US
dc.rights.holderCopyright © 2001 by The Endocrine Societyen_US

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