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  • Title: Oestrogen receptor components of human endometrium.
    Author: Braunsberg H, Pflaeger JE.
    Journal: J Steroid Biochem; 1981 Dec; 15():313-6. PubMed ID: 7339258.
    Abstract:
    The investigation was undertaken in order to demonstrate the existence of 2 species of receptor in cytosol and nuclear preparations and to examine their relative stability under conditions necessary to effect exchange of endogenous bound steroid. The methods used for tissue fractionation and receptor analysis have been published and are outlined in figures. Cystol preparations corresponding to 100 mg tissue per ml buffer were used for experiments with [2,4,6,7-3H]-estradiol ([3H]-E2,SA 93/Ci/mmol); further 5-fold dilutions were made when 16x-[1251]-estradiol ([25I]-E2, initial SA1000 Ci/mmol) was used. Washed nuclear pellets [I] were taken up in volumes of buffer corresponding to 400 mg and 100 mg tissue per ml in experiments with [3H]-E2 and [125I]-E2, respectively. On warming at 40 degrees Celsius 2 species of low capacity estradiol binding sites can be distinguished in preparations from human endometrium: a labile form which is destroyed within 20 or 30 minutes and a more stable form which is lost more slowly at this temperature. Both types are stable at 4 and 15 degrees Celsius but 1 is highly labile at 30 degrees Celsius and above. Both types are stable in cystol preparations at 22 degrees Celsius at which temperature estradiol dissociates from receptor complexes. In nuclear preparations the more labile form is lost rapidly during exchange at 22 degrees Celsius. The presence of KC1 in nuclear homogenates reduced binding of estradiol to both forms of receptor. The existence of 2 distinguishable types of high affinity binding sites in human endometrial nuclei raises the issue as to whether they serve different functions in the biological actions of estrogen, and this possibility should be further investigated.
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