• Login
    View Item 
    •   Shocker Open Access Repository Home
    • Fairmount College of Liberal Arts and Sciences
    • Biological Sciences
    • BIO Faculty Scholarship
    • BIO Faculty Publications
    • View Item
    •   Shocker Open Access Repository Home
    • Fairmount College of Liberal Arts and Sciences
    • Biological Sciences
    • BIO Faculty Scholarship
    • BIO Faculty Publications
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Comparative glycomics of the glycoprotein follicle stimulating hormone: glycopeptide analysis of isolates from two mammalian species

    Date
    2006-06-21
    Author
    Dalpathado, Dilusha S.
    Irungu, Janet
    Go, Eden P.
    Butnev, Vladimir Y.
    Norton, Katie
    Bousfield, George R.
    Desaire, Heather
    Metadata
    Show full item record
    Citation
    Dalpathado 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):8665-73
    Abstract
    Follicle 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.
    Description
    Click on the DOI link to access this article
    URI
    http://dx.doi.org/10.1021/bi060435k
    http://hdl.handle.net/10057/5985
    Collections
    • BIO Faculty Publications

    Browse

    All of Shocker Open Access RepositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsBy TypeThis CollectionBy Issue DateAuthorsTitlesSubjectsBy Type

    My Account

    LoginRegister

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    DSpace software copyright © 2002-2023  DuraSpace
    DSpace Express is a service operated by 
    Atmire NV