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dc.contributor.authorChapman, A J
dc.contributor.authorGallagher, John T
dc.contributor.authorBeardwell, Colin G
dc.contributor.authorShalet, Stephen M
dc.date.accessioned2011-03-12T23:52:03Z
dc.date.available2011-03-12T23:52:03Z
dc.date.issued1984-10
dc.identifier.citationLack of binding of serum glycoprotein hormone alpha subunit to concanavalin A-Sepharose reflects increased branching of the oligosaccharide chains. 1984, 103 (1):111-6 J Endocrinolen
dc.identifier.issn0022-0795
dc.identifier.pmid6207258
dc.identifier.doi10.1677/joe.0.1030111
dc.identifier.urihttp://hdl.handle.net/10541/124419
dc.description.abstractThe lectin-binding properties of serum alpha subunit were studied by lectin affinity chromatography. Normal individuals and most patients with pituitary tumours produced alpha subunit which bound specifically to Concanavalin A-Sepharose (Con A). Some patients with pituitary tumours produced both Con A-reactive alpha subunit and alpha subunit which did not bind to Con A. Concanavalin A-Sepharose-binding alpha subunit from all sources bound strongly to Ricinus communis agglutinin-Sepharose after treatment with neuraminidase. Serum alpha subunit from those patients with pituitary tumours, which did not bind to Con A, bound to wheat germ agglutinin-Sepharose, exhibiting both weakly binding and strongly binding forms. Serum alpha subunit from both patients and controls, which did bind to Con A, showed only weak affinity for wheat germ agglutinin-Sepharose. Neither the low affinity nor the high affinity of serum alpha subunit from any source for wheat germ agglutinin-Sepharose was affected by neuraminidase. These findings show that (a) the predominant pattern of glycosylation of serum alpha subunit from normal controls is a Con A-reactive, biantennate complex oligosaccharide and (b) that the structural alteration which results in serum alpha subunit which does not bind to Con A in some patients with pituitary tumours is not an absence of carbohydrate, rather the alpha subunit contains highly branched, either complex or hybrid oligosaccharides.
dc.language.isoenen
dc.subject.meshAdult
dc.subject.meshChromatography, Affinity
dc.subject.meshChromatography, Gel
dc.subject.meshChromatography, Ion Exchange
dc.subject.meshConcanavalin A
dc.subject.meshFemale
dc.subject.meshGlycoprotein Hormones, alpha Subunit
dc.subject.meshHumans
dc.subject.meshLectins
dc.subject.meshMale
dc.subject.meshMiddle Aged
dc.subject.meshOligosaccharides
dc.subject.meshPeptide Fragments
dc.subject.meshPituitary Hormones, Anterior
dc.subject.meshPituitary Neoplasms
dc.subject.meshPlant Lectins
dc.subject.meshProtein Binding
dc.subject.meshSepharose
dc.subject.meshWheat Germ Agglutinins
dc.titleLack of binding of serum glycoprotein hormone alpha subunit to concanavalin A-Sepharose reflects increased branching of the oligosaccharide chains.en
dc.typeArticleen
dc.contributor.departmentPaterson Laboratories and Radiotherapy Department, CHristie Hospital and Holt Radium Institute, Manchester M20 9BXen
dc.identifier.journalThe Journal of Endocrinologyen
html.description.abstractThe lectin-binding properties of serum alpha subunit were studied by lectin affinity chromatography. Normal individuals and most patients with pituitary tumours produced alpha subunit which bound specifically to Concanavalin A-Sepharose (Con A). Some patients with pituitary tumours produced both Con A-reactive alpha subunit and alpha subunit which did not bind to Con A. Concanavalin A-Sepharose-binding alpha subunit from all sources bound strongly to Ricinus communis agglutinin-Sepharose after treatment with neuraminidase. Serum alpha subunit from those patients with pituitary tumours, which did not bind to Con A, bound to wheat germ agglutinin-Sepharose, exhibiting both weakly binding and strongly binding forms. Serum alpha subunit from both patients and controls, which did bind to Con A, showed only weak affinity for wheat germ agglutinin-Sepharose. Neither the low affinity nor the high affinity of serum alpha subunit from any source for wheat germ agglutinin-Sepharose was affected by neuraminidase. These findings show that (a) the predominant pattern of glycosylation of serum alpha subunit from normal controls is a Con A-reactive, biantennate complex oligosaccharide and (b) that the structural alteration which results in serum alpha subunit which does not bind to Con A in some patients with pituitary tumours is not an absence of carbohydrate, rather the alpha subunit contains highly branched, either complex or hybrid oligosaccharides.


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