Characterization of the membranous antiestrogen binding protein: I. Partial purification of the protein in its active state
| Autor: | Fabienne Mésange, Marc Poirot, Jean-Charles Faye, Francis Bayard, Catherine Chailleux |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Receptors
Drug Estrogen receptor Breast Neoplasms Biology Rats Sprague-Dawley Native state Animals Binding site Phospholipids Pharmacology Sequence Homology Amino Acid Chromatofocusing Binding protein Uterus Reproducibility of Results Antiestrogen Ligand (biochemistry) Rats Isoelectric point Biochemistry Liver Solubility Organ Specificity Female Isoelectric Focusing Ultracentrifugation |
| Zdroj: | Journal of receptor research. 14(1) |
| ISSN: | 0197-5110 |
| Popis: | 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 reported 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. |
| Databáze: | OpenAIRE |
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