Skip to Main content Skip to Navigation
Journal articles

Characterization of the membranous antiestrogen binding protein: I. Partial purification of the protein in its active state.

Abstract : We previously demonstrated that, in addition to the estrogen receptor, the Antiestrogen Binding Site (ABS) is also a potent mediator of the antitumorous activity of the clinical drug tamoxifen. Because of report discrepancies in the binding parameters of rat liver ABS we first attempted to improve binding study conditions. In this way buffer, protein concentration, methodology for bound/free ligand separation and phospholipidic ratio were determined. This work was used to evaluate the Stoke radius (4.4 S) and isoelectric point (pH = 6.6) of the protein in its native state. These studies constituted the obligatory transition from rat liver to pure ABS protein.
Document type :
Journal articles
Complete list of metadatas

https://www.hal.inserm.fr/inserm-00090795
Contributor : Marc Poirot <>
Submitted on : Monday, September 4, 2006 - 1:22:56 AM
Last modification on : Monday, September 4, 2006 - 3:57:06 PM

Identifiers

  • HAL Id : inserm-00090795, version 1
  • PUBMED : 8158580

Collections

Citation

Catherine Chailleux, Marc Poirot, Fabienne Mésange, Francis Bayard, Jean-Charles Faye. Characterization of the membranous antiestrogen binding protein: I. Partial purification of the protein in its active state.. J Recept Res, 1994, 14, pp.23-35. ⟨inserm-00090795⟩

Share

Metrics

Record views

164