Abstract
The soluble receptor-estrogen complexes from mature rat uteri, which sediment in the 9-S region of sucrose gradients, are reversibly dissociated into two dissimilat units (A and B) when exposed to 0.3 M KCl; only the A unit binds estradiol. Partial separation of the units is obtained by sedimentation through sucrose gradients and by gel filtration on 6% agarose, columns. Aging the receptors in the presence of 0.3 M KCl at 0° prevents the reassociation of the subunits when they are sedimented into gradients lacking KCl. A small subunit (C) appears to be released from its original association within the 9-S complex during the aging process. This unit, which can be extracted with 0.3 M KCl from receptor complexes adsorbed on PVM-estradiol resin, modifies the A units and prevents them from reassociating with intact B units. A possible role of the modified receptors in the mechanism of estrogen action is discussed.
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