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Title: Different interaction of estradiol and antiestrogens with the estrogen receptor of rat uterus. Author: Faye JC, Fargin A, Bayard F. Journal: Mol Cell Endocrinol; 1986 Sep; 47(1-2):119-24. PubMed ID: 3743888. Abstract: Cytosoluble estradiol-receptor (ER) complexes obtained from uteri of castrated rats show a 4.3 S sedimentation coefficient when analysed by sucrose gradient in high salt buffer both in the absence and presence of 0.1 M ammonium thiocyanate. After incubation with nuclei, the complexes sediment at 4.3 S and at 3.2 S, in the absence and presence of 0.1 M ammonium thiocyanate respectively. This structural modification of ER is also confirmed by gel filtration analysis. In similar conditions hydroxytamoxifen-ER complexes apparently do not undergo such a modification. However, increasing the molarity of the chaotropic ion up to 0.5 M shows that, in fact, the modification occurs. Sodium dodecylsulfate-polyacrylamide gel electrophoresis analysis of covalently linked tamoxifen aziridine-ER 'complexes' confirms that the nuclear treatment reduces the apparent molecular weight of ER from 62 000 to 47 000. These data demonstrate that, in vitro, nuclear ER is cleaved into a smaller molecular form and that the receptor fragments can be held together by the triphenylethylene antiestrogen hydroxytamoxifen.[Abstract] [Full Text] [Related] [New Search]