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dc.contributor.authorChapman, A Jen
dc.contributor.authorGallagher, John Ten
dc.contributor.authorBeardwell, Colin Gen
dc.contributor.authorShalet, Stephen Men
dc.date.accessioned2011-03-12T23:43:17Z
dc.date.available2011-03-12T23:43:17Z
dc.date.issued1984-10
dc.identifier.citationVariation in the core and branch carbohydrate sequences of serum glycoprotein hormone alpha subunit as determined by lectin affinity chromatography. 1984, 103 (1):117-22 J Endocrinolen
dc.identifier.issn0022-0795
dc.identifier.pmid6207259
dc.identifier.doi10.1677/joe.0.1030117
dc.identifier.urihttp://hdl.handle.net/10541/124418
dc.description.abstractSerum alpha subunits from patients with pituitary tumours and from normal controls were studied for their ability to bind to Lens culinaris agglutinin-Sepharose (LCA), L-phytohaemagglutinin-agarose (L-PHA) and soybean agglutinin-Sepharose (SBA). Serum alpha subunits from normal controls which had previously been shown to bind to Concanavalin A-Sepharose (Con A) were not retained by LCA. In contrast, Con A-reactive alpha subunits from patients with pituitary tumours bound specifically to LCA. Non-Con A-reactive alpha subunits from patients with pituitary tumours were also largely not bound to LCA, but were retained by L-PHA. No alpha subunits from any source bound to SBA. These results indicate that the structural alterations resulting in non-Con A-reactive serum alpha subunits include highly branched complex oligosaccharides in addition to the hybrid-type glycans previously described. The increased branching appears to be associated with fucosylation in the core region of the oligosaccharides. Serum alpha subunit from any source appears to be devoid of terminal N-acetylgalactosamine residues. These structural modifications may be related to the variable biological activity of alpha subunit which has been reported.
dc.language.isoenen
dc.subject.meshCarbohydrate Sequence
dc.subject.meshChromatography, Affinity
dc.subject.meshFemale
dc.subject.meshGlycoprotein Hormones, alpha Subunit
dc.subject.meshHumans
dc.subject.meshLectins
dc.subject.meshMiddle Aged
dc.subject.meshOligosaccharides
dc.subject.meshPeptide Fragments
dc.subject.meshPituitary Hormones, Anterior
dc.subject.meshPituitary Neoplasms
dc.subject.meshProtein Binding
dc.titleVariation in the core and branch carbohydrate sequences of serum glycoprotein hormone alpha subunit as determined by lectin affinity chromatography.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.abstractSerum alpha subunits from patients with pituitary tumours and from normal controls were studied for their ability to bind to Lens culinaris agglutinin-Sepharose (LCA), L-phytohaemagglutinin-agarose (L-PHA) and soybean agglutinin-Sepharose (SBA). Serum alpha subunits from normal controls which had previously been shown to bind to Concanavalin A-Sepharose (Con A) were not retained by LCA. In contrast, Con A-reactive alpha subunits from patients with pituitary tumours bound specifically to LCA. Non-Con A-reactive alpha subunits from patients with pituitary tumours were also largely not bound to LCA, but were retained by L-PHA. No alpha subunits from any source bound to SBA. These results indicate that the structural alterations resulting in non-Con A-reactive serum alpha subunits include highly branched complex oligosaccharides in addition to the hybrid-type glycans previously described. The increased branching appears to be associated with fucosylation in the core region of the oligosaccharides. Serum alpha subunit from any source appears to be devoid of terminal N-acetylgalactosamine residues. These structural modifications may be related to the variable biological activity of alpha subunit which has been reported.


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