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Biology of Reproduction, Vol 12, 134-142, Copyright © 1975 by Society for the Study of Reproduction
1 Department of Cell Biology, Baylor College of Medicine, Houston, Texas 77025 A 6S progesterone receptor form has been identified in chick oviduct cytosol fractions. It has been
shown to consist of equal amounts of two 4S receptor subunits, A and B, previously shown to bind in
nuclei to DNA and chromatin sites respectively. The 6S form is tentatively defined as a dimer of both A
and B subunits. It is present in cytosol under conditions in which large in vitro aggregate formation (8S)
is prevented. The 6S dimer co-chromatographs with authentic receptor B on DEAE-cellulose, but does
not bind to phosphocellulose. Dissociation of the dimer with salt or temperature liberates the receptor
subunits in their monomeric 4S forms.
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