Estrogen and antiestrogen binding to different forms of the molybdate-stabilized estrogen receptor

Mary F. Ruh, Robert G. Brzyski, Lynn Strange, Thomas S. Ruh

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

We report that the calf uterine estrogen receptor, prepared in a Tris-raolybdate buffer, bound by 10 nM [3H]estradiol and eluted by a KCl gradient from DEAE-cellulose columns, yielded only one very sharp receptor peak. Estrogen receptor prepared in phosphate buffer with molybdate and eluted with KCl also yielded only one sharp peak on DEAE-cellulose. However, if DEAE-Sephadex (with phosphate buffer plus molybdate) was used, the [3H]estradiol-receptor complex eluted with two sharp peaks at approximately 0.21 and 0.25 M KCl (Peaks I and II, respectively). But the high-affinity antiestrogen, [3H]H1285, bound to estrogen receptor, eluted only as Peak I and not as Peak II. Both the [3H]estradiol and [3H]H1285 binding peaks were saturable since they could be eliminated with 200-fold excess estradiol. Therefore, ion exchangechromatography using different resins and/or buffers may be useful for determining physicochemicai differences in estrogen versus antiestrogen receptor complexes.

Original languageEnglish (US)
Pages (from-to)2203-2205
Number of pages3
JournalEndocrinology
Volume112
Issue number6
DOIs
StatePublished - Jun 1983
Externally publishedYes

ASJC Scopus subject areas

  • Endocrinology

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