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Title

Purification and characterization of follicle-stimulating hormone from pituitary glands of sea bass (Dicentrarchus labrax)

AuthorsMolés, Gregorio ; Gómez, Ana ; Rocha, Ana; Carrillo, Manuel ; Zanuy, Silvia
Issue Date2008
PublisherAcademic Press
CitationGeneral and Comparative Endocrinology 158(1): 68-76 (2008)
AbstractFollicle-stimulating hormone (FSH) was purified from pituitaries of sea bass (Dicentrarchus labrax), and its biochemical and biological properties were studied. Sea bass FSH (sbsFSH) was purified by ethanol extraction-precipitation (40-85%), followed by anion-exchange chromatography on a LKB Ultropac TSK-DEAE column using a linear gradient of ammonium bicarbonate (50-1000 mM) and reverse phase chromatography on a RESOURCE 15RPC column with a linear gradient of acetonitrile (0-50%), using a FPLC system. The molecular mass of the purified sbsFSH, estimated by mass spectrometry, was of 28.5 kDa for the dimer, 12.6 kDa for the glycoprotein α (GPα) and 13.6 kDa for FSHβ subunits. After separation by SDS-PAGE under reducing condition, the intact sbsFSH was dissociated in the respective subunits (GPα and FSHβ). Subunit identity was confirmed by immunological detection and N-terminal amino acid sequencing. Deglycosylation treatment with N-glycosidase F, decreased the molecular mass of both subunits. Intact sbsFSH activated the sea bass FSH receptor stably expressed in the cell line HEK 293, in a dose dependent manner. Purified sbsFSH showed gonadotropic activity, by stimulating the release of estradiol-17β (E2) from sea bass ovary and testosterone (T) and 11-ketotestosterone (11KT) from testicular tissue cultured in vitro, in a dose and time dependent manner. These results showed that the purified sbsFSH is a heterodimeric hormone, composed of two distinct glycoprotein subunits (GPα and FSHβ), and has biological activity judged by its ability to stimulate its receptor in a specific manner and to promote steroid release from gonadal tissue fragments. © 2008 Elsevier Inc. All rights reserved.
URIhttp://hdl.handle.net/10261/72129
DOI10.1016/j.ygcen.2008.05.005
Identifiersdoi: 10.1016/j.ygcen.2008.05.005
issn: 0016-6480
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