Sea bass ( Dicentrarchus labrax L.) vitellogenin. I—Induction, purification and partial characterization
Identifieur interne : 001C18 ( Main/Merge ); précédent : 001C17; suivant : 001C19Sea bass ( Dicentrarchus labrax L.) vitellogenin. I—Induction, purification and partial characterization
Auteurs : E. Ma An S [Espagne] ; S. Zanuy [Espagne] ; Françoise Le Menn [France] ; M. Carrillo [Espagne] ; J. Nú EzSource :
- Comparative Biochemistry and Physiology, Part B: Biochemistry and Molecular Biology [ 0305-0491 ] ; 1994.
Abstract
In sea bass (males and non-vitellogenic females) estradiol (E2) treatment caused the appearance in the bloodstream of a new protein that was identified as the vitellogenin (VTG) molecule for this teleost species. The molecular weight of the sea bass VTG (445 kDa) and its amino acid composition was similar to that of other teleosts. VTG was purified by double-step chromatography and then used to obtain specific antibodies. The localization of VTG in the liver and in the ovary was carried out by immunocytochemistry. The effects of the E2 treatment on the synthetic activity of the liver were studied throughout the modifications observed at the histological and biochemical levels.
Url:
DOI: 10.1016/0305-0491(94)90041-8
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Zanuy</name></author><author><name sortKey="Le Menn, F" sort="Le Menn, F" uniqKey="Le Menn F" first="F." last="Le Menn">Françoise Le Menn</name><affiliation><country>France</country><placeName><settlement type="city">Bordeaux</settlement><region type="region" nuts="2">Nouvelle-Aquitaine</region><region type="old region" nuts="2">Aquitaine</region></placeName><orgName type="university" n="3">Université Bordeaux I</orgName><orgName type="institution" wicri:auto="newGroup">Université de Bordeaux</orgName></affiliation></author><author><name sortKey="Carrillo, M" sort="Carrillo, M" uniqKey="Carrillo M" first="M." last="Carrillo">M. Carrillo</name></author><author><name sortKey="Nu Ez, J" sort="Nu Ez, J" uniqKey="Nu Ez J" first="J." last="Nú Ez">J. 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The molecular weight of the sea bass VTG (445 kDa) and its amino acid composition was similar to that of other teleosts. VTG was purified by double-step chromatography and then used to obtain specific antibodies. The localization of VTG in the liver and in the ovary was carried out by immunocytochemistry. The effects of the E2 treatment on the synthetic activity of the liver were studied throughout the modifications observed at the histological and biochemical levels.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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