Abstract
Homogenization of rat uteri at 25°C resulted in a particulate partitioning of the estrogen receptor. Homogenization at 0°C, the use of frozen tissue, or the pre-exeposure of the tissue to 0°C prior to 25°C homogenization induced soluble partitioning of the estrogen receptor. Binding of a radiolabeled monoclonal antibody indicated that, in absence of estradiol, the estrogen receptor is particulate and is associated with the nuclei-enriched fraction of the target cell. The presence of receptor in the soluble fraction thus appears to be an artifact of homogenization. The unoccupied receptor, loosely associated with the particulate fraction (cold-sensitive) represents the “native” form of receptor which, upon arrival of the hormone, becomes tightly associated (cold-insensitive). The transition from the cold-sensitive to the cold-insensitive status is accompanied by a modification of the electrical charge of the receptor.
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