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Departments of Medicine and Obstetrics and Gynecology, Vanderbilt University School of Medicine Nashville, Tennessee 37232
Abstract
An estradiol binding component has been identified in the cytoplasmic fraction of the immature chick oviduct. The method used to resolve this receptor differed from the standard sucrose gradient centrifugation approach in that tritiated hormone was present throughout the sucrose gradient. This modification was necessary to preserve the hormone complex during centrifugation. Under these conditions, an
8 S binding component was demonstrated which underwent dissociation to a
5 S component in high ionic strength medium. Binding specificity determinations revealed that this receptor preferentially bound estrogens. Quantitative binding analysis showed that a limited class of binding sites was present with a dissociation constant (Kd) for estradiol of
8.6 x 10–10M. These properties indicate that this binding component may function as a biologic receptor for estrogens in the oviduct. (Endocrinology 96: 199, 1975)
Footnotes
* This work was supported by NIH contract 70-2165, NIH Grants 05697, 5-TOI-AM-05092 and the Vanderbilt Research Council.
1 Josiah Macy, Jr., Faculty Fellow.
2 To whom requests for reprints should be directed.
3 Present address: Department of Endocrine Research, Mayo Clinic, Rochester, Minnesota 55901.
Received April 15, 1974.
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