Abstract

Chicken oviduct progesterone receptor in cytosol was found to be transformed from the 8S to 4S form by incubation at 25°C as well as by 0.3 M KCl in the absence of hormone. Heat transformation of ligand-free receptor took place at a much slower rate than that of ligand-bound reeceptor. The eventual percentage of transformation, however, was almost the same. The 4S form of the receptor transformed by KCl in the absence of hormone could bind to DNA-cellulose, but not to nuclei. However, upon exposure it acquired the ability to bind to nuclei. It was shown that the transformed ligand-free receptor could bind to progesterone to form the normal activated steroid-receptor complex. Conversely, when activated 4S progesterone-receptor complex was treated with DCC to peel off the hormone, a resulting ligand-free receptor was formed which behaved just like the KCl-transformed receptor in the absence of hormone.

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