Endocrinology, Vol 112, 2203-2205, Copyright © 1983 by Endocrine Society

ARTICLES

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

MF Ruh, RG Brzyski, L Strange and TS Ruh

We report that the calf uterine estrogen receptor, prepared in a Tris- molybdate 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 exchange chromatography using different resins and/or buffers may be useful for determining physicochemical differences in estrogen versus antiestrogen receptor complexes.

This article has been cited by other articles:

				C. Grossman Interactions between the gonadal steroids and the immune system Science, January 18, 1985; 227(4684): 257 - 261. [Abstract] [PDF]