The selective isolation of the uterine oestradiol-receptor complex by binding to oligo(dT)-cellulose. The mediation of an essential activator in the transformation of cytosol receptor.

The selective isolation of the uterine oestradiol-receptor complex by binding to oligo(dT)-cellulose. The mediation of an essential activator in the transformation of cytosol receptor.
复制标题

通过与寡 (dT)-纤维素结合选择性分离子宫雌二醇受体复合物。

DOI:
10.1042/bj1600271
复制
发表时间:
1976
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
Miriam Marks
Miriam Marks
中科院分区:
--
文献类型:
--
作者:
C. Hall;L. Lim;A. Davison;Miriam Marks

文献摘要

被引文献

相似文献

用寡聚(DT)-纤维素柱层析从大鼠子宫胞浆中选择性地分离出[~3H]雌二醇-受体复合体。描述了该络合物与寡聚(DT)-纤维素结合的最佳条件,这与其与DNA-纤维素的结合相似。胞浆复合体有一个明显的摩尔。经Sephadex G-100层析测定,在高盐浓度下重量为50,000-60,000。这相当于细胞质中的4S雌二醇受体。在与寡聚(DT)-纤维素结合时,受体转变为具有明显摩尔质量的形式。100,000-120,000,对应于5S核受体复合体。这种转变模仿了体内细胞质雌激素受体转化为核形式的过程。明确地证明,该络合物与寡聚(DT)-纤维素作为5S核形式的结合需要胞浆中存在的活化物质的调节。关于雌二醇-受体复合体的核结合不仅仅由细胞质雌二醇受体的可用性决定的报道,对激活因子的要求进行了讨论。
The [3H]oestradiol-receptor complex was selectively isolated from rat uterus cytosol by column chromatography on oligo(dT)-cellulose. Optimal conditions are described for the binding of the complex to oligo(dT)-cellulose, which is shown to be similar to its binding to DNA-cellulose. The cytosol complex has an apparent mol. wt. of 50,000-60,000 in high salt concentrations, as determined by Sephadex G-100 chromatography. This corresponds to the 4S cytoplasmic oestradiol receptor. In binding to oligo(dT)-cellulose the receptor is transformed into a form with an apparent mol.wt. of 100,000-120,000, corresponding to the 5S nuclear receptor complex. This transformation mimics the conversion in vivo of the cytoplasmic oestradiol receptor into the nuclear form. The binding of the complex to oligo(dT)-cellulose as a 5S nuclear form is unequivocally demonstrated to require the mediation of an activating present in the cytosol. The requirement for an activating factor is discussed in relation to reports that nuclear binding of the oestradiol-receptor complex is not dictated solely by the availability of the cytoplasmic oestradiol receptor.