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dc.contributor.authorDalpathado, Dilusha S.
dc.contributor.authorIrungu, Janet
dc.contributor.authorGo, Eden P.
dc.contributor.authorButnev, Vladimir Y.
dc.contributor.authorNorton, Katie
dc.contributor.authorBousfield, George R.
dc.contributor.authorDesaire, Heather
dc.date.accessioned2013-07-18T18:34:43Z
dc.date.available2013-07-18T18:34:43Z
dc.date.issued2006-06-21
dc.identifier.citationDalpathado DS, Irungu J, Go EP, Butnev VY, Norton K, Bousfield GR, Desaire H; Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species; Biochemistry. 2006 Jul 18;45(28):8665-73en_US
dc.identifier.issn0006-2960 (Print)
dc.identifier.urihttp://dx.doi.org/10.1021/bi060435k
dc.identifier.urihttp://hdl.handle.net/10057/5985
dc.descriptionClick on the DOI link to access this articleen_US
dc.description.abstractFollicle stimulating hormone (FSH) is one of the important hormones that regulate gonadal functions. This hormone is glycosylated, and the glycans greatly influence the biological properties. In the present study the negatively charged glycopeptides of equine and human pituitary follicle stimulating hormone (eFSH and hFSH) have been characterized in a glycosylation site-specific manner using FT-ICR-MS and Edman sequencing. The characteristic pattern of glycan distribution at each glycosylation site has been deduced and compared between horse and human FSH preparations. The data suggest that site-specific differences exist between glycoforms of human and equine FSH. For instance, except for one site in the β subunit (Asn7) of hFSH all other sites in both species have sulfated glycoforms. Also, glycoforms at Asn52 of hFSH are all complex type, whereas in eFSH, both complex and hybrid structures exist at this site. There is also a higher percentage of sulfated glycans in the latter site compared to the former. This is the first study that characterizes the glycans from this hormone in a glycosylation site-specific manner, and these data can be used to begin correlative studies between glycosylation structure and hormone function.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofseriesBiochemistry;
dc.relation.ispartofseries;V.45, No.28
dc.titleComparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian speciesen_US
dc.typeArticleen_US


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