Abstract
This chapter describes hormone-induced transformation of receptor proteins. During the course of steroid-induced translocation to the nuclei of their respective target cells, extra nuclear receptor proteins for estrogenic and androgenic hormones undergo temperature-dependent alteration that can be recognized both by a change in sedimentation properties and the acquisition of an ability to bind to isolated nuclei or chromatin. Warming the uterine cytosol receptor with estradiol increases the sedimentation coefficient of the complex from 3–8 S to 5–3 S, whereas similar incubation of the prostatic cytosol receptor with dihydrotestosterone decreases the sedimentation coefficient from 3–8 S to 3–0 S. Treatment of isolated uterine nuclei with transformed estradiol–receptor complex not only increases their RNA polymerase activity but also changes the nearest neighbor frequency spectrum of the RNA produced, in the same manner as does estradiol administered in vivo.
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