Positive cooperativity of the estrogen receptor.
Positive cooperativity of the estrogen receptor.
复制标题
雌激素受体的正协同作用。
DOI：
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发表时间：
1981
影响因子：
11.1
通讯作者：
D. E. Hamilton
中科院分区：
文献类型：
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作者：
A. Notides;N. Lerner;D. E. Hamilton
在25 ℃下测定小牛子宫部分纯化的雌激素受体与[3 H]雌二醇的平衡结合。结合数据的Scatchard图显示了正协同性的凸曲线特征，在1至10 nM的受体浓度下，Hill系数为1.58 +/- 0.21。低于约0.3 nM的受体浓度的Scatchard图接近线性，这表明合作的相互作用是依赖于单体-二聚体平衡。胰蛋白酶预处理的受体导致损失的二聚体形成和合作的相互作用。雌激素受体的积极合作的特点是不产生的受体失活，未能完成[3 H]雌二醇-受体平衡反应，或放射性杂质的[3 H]雌二醇。这些结果表明，激活的5S雌激素受体是一个同源二聚体，它的形成与正合作雌二醇结合反应。
The equilibrium [3H]estradiol binding by the partially purified estrogen receptor from calf uteri was measured at 25 degrees C. The Scatchard plot of the binding data showed a convex curve characteristic of positive cooperativity and a Hill coefficient of 1.58 +/- 0.21, at receptor concentrations of 1 to 10 nM. Below a receptor concentration of approximately 0.3 nM the Scatchard plot approached linearity, suggesting that the cooperative interactions are dependent upon a monomer--dimer equilibrium. Trypsin pretreatment of the receptor resulted in a loss of dimer formation and of the cooperative interactions. The positive cooperative characteristics of the estrogen receptor were shown not to be produced by receptor inactivation, failure to complete the [3H]estradiol--receptor equilibrium reaction, or radioimpurity of the [3H]estradiol. These findings indicate that the activated 5S estrogen receptor is a homodimer and that its formation is associated with a positive cooperative estradiol-binding reaction.