Dickson R B, Aten R F, Eisenfeld A J
Endocrinology. 1978 Nov;103(5):1636-46. doi: 10.1210/endo-103-5-1636.
Mature male rat liver cytosol contains a moderate affinity and capacity estrogen-binding protein in at least a 200-fold higher level than mature female or immature male rat liver cytosol. Binding of estradiol to this protein is very rapid, is stabilized by EDTA, and is inhibited by divalent cations. This is the major binding protein for [3H]estradiol ([3H]E2) in mature male rat liver cytosol, and it has properties clearly distinguishing it from putative liver or uterine estrogen receptors. In addition to binding [3H]E2, this protein seems to rapidly bind a [3H]5alpha-dihydrotestosterone ([3H]DHT) metabolite at the same binding site. The binding of this androgen metabolite is stabilized by EDTA and is inhibited by divalent cations. The binding properties of the [3H]DHT metabolite suggest that these binding sites are not classical androgen receptors. Cytosol binding levels of both the [3H]E2 and the [3H]DHT metabolites change in a similar direction in resonse to endocrine manipulation. The putative liver estrogen receptor level, determined after partial purification (in a redissolved 30% ammonium sulfate-precipitated fraction), seems to change in an opposite direction in response to these same endocrine manipulations.
成熟雄性大鼠肝脏胞质溶胶含有一种中等亲和力和容量的雌激素结合蛋白，其水平至少比成熟雌性或未成熟雄性大鼠肝脏胞质溶胶高200倍。雌二醇与该蛋白的结合非常迅速，可被EDTA稳定，并受到二价阳离子的抑制。这是成熟雄性大鼠肝脏胞质溶胶中[3H]雌二醇（[3H]E2）的主要结合蛋白，其特性明显不同于假定的肝脏或子宫雌激素受体。除了结合[3H]E2外，该蛋白似乎还能在同一结合位点快速结合一种[3H]5α-二氢睾酮（[3H]DHT）代谢物。这种雄激素代谢物的结合可被EDTA稳定，并受到二价阳离子的抑制。[3H]DHT代谢物的结合特性表明这些结合位点不是经典的雄激素受体。[3H]E2和[3H]DHT代谢物的胞质溶胶结合水平在对内分泌调节的反应中变化方向相似。经部分纯化（在重新溶解的30%硫酸铵沉淀级分中）后测定的假定肝脏雌激素受体水平，在对这些相同内分泌调节的反应中似乎变化方向相反。
