Harrison R W, Toft D O
Endocrinology. 1975 Jan;96(1):199-205. doi: 10.1210/endo-96-1-199.
An estradiol binding component has been identified in the cytoplasmic fraction of the immature chick oviduct. The method used to resolve this receptor differed from the standard sucrose gradient centrifugation approach in that tritiated hormone was present throughout the sucrose gradient. This modification was necessary to preserve the hormone complex during centrifugation. Under these conditions, an similar to 8 S binding component was demonstrated which underwent dissociation to a similar to 5 S component in high ionic strength medium. Binding specificity determinations revealed that this receptor preferentially bound estrogens. Quantitative binding analysis showed that a limited class of binding sites was present with a dissociation constant (K-d) for estradiol of similar to 8.6 times 10-10M. These properties indicate that this binding component may function as a biologic receptor for estrogens in the oviduct.
在未成熟雏鸡输卵管的细胞质部分已鉴定出一种雌二醇结合成分。用于分离该受体的方法与标准蔗糖梯度离心法不同，因为在整个蔗糖梯度中都存在氚标记的激素。这种改进对于在离心过程中保存激素复合物是必要的。在这些条件下，证明了一种类似于8S的结合成分，在高离子强度介质中它会解离为类似于5S的成分。结合特异性测定表明该受体优先结合雌激素。定量结合分析表明存在一类有限的结合位点，其对雌二醇的解离常数（K-d）约为8.6×10-10M。这些特性表明该结合成分可能作为输卵管中雌激素的生物受体发挥作用。
