Molecular properties of the androgen receptor in rat ventral prostate.
Molecular properties of the androgen receptor in rat ventral prostate.
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大鼠腹侧前列腺雄激素受体的分子特性。
DOI：
10.1111/j.1749-6632.1984.tb38274.x
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发表时间：
1984
影响因子：
5.2
通讯作者：
Rowley,DR
中科院分区：
文献类型：
--
作者：
Tindall,DJ;Chang,CH;Lobl,TJ;Rowley,DR
从这些研究的结果表明，我们已经从大鼠前列腺细胞质中纯化了一种蛋白质，它与β-蛋白质相似（复合物II），但不同于α-蛋白纯化的受体与雄激素结合蛋白（ABP）的不同之处在于ABP具有更快的解离速率（6 min）、更低的pI值、更高的亲和力和更高的亲和力。（4.6），并且需要比前列腺雄激素受体更高浓度的硫酸铵沉淀（40-50%）。这是不可能的，我们已经纯化了血清性类固醇结合蛋白，因为没有这样的蛋白在大鼠血清中发现。本文报道了一种从大鼠前列腺腹侧提取雄激素受体的快速、有效的方法。然而，目前的方法只允许我们从每种制剂中获得有限数量的纯化受体。很明显，我们需要扩大受体的纯化，以详细研究其物理化学性质，并产生针对蛋白质的单特异性抗体。这项工作正在进行中。此外，我们已经证明，两个亲和标记可用于共价结合的雄激素受体。最重要的是，这些化合物可用于在非变性和变性条件下表征雄激素受体，并代表了将来一般使用雄激素受体蛋白和雄激素相关蛋白的有用工具。
Results from these studies demonstrate that we have purified a protein from rat prostate cytosol that is similar to the beta-protein (complex II) but different from the alpha-protein (complex I) reported by Liao et al. The purified receptor was different from androgen binding protein (ABP) in that ABP has a faster dissociation rate (6 min), a lower pI value (4.6), and requires higher concentrations of ammonium sulfate for precipitation (40-50%) than the prostatic androgen receptor. It is not likely that we have purified a serum sex-steroid binding protein since no such protein is found in rat serum. This report presents a rapid and efficient procedure for the purification of androgen receptor from rat ventral prostate. However, the present procedure only allowed us to obtain a limited quantity of purified receptor from each preparation. It is obvious that we need to scale up the purification of the receptor in order to study in detail its physicochemical properties and to produce monospecific antibodies against the protein. This work is in progress. In addition, we have demonstrated that two affinity labels can be used to bind covalently to the androgen receptor. Most importantly, these compounds can be used to characterize androgen receptors under both nondenaturing and denaturing conditions and represent useful tools for future work with androgen receptor proteins and androphilic proteins in general.