Schrader W T, O'Malley B W
Adv Exp Med Biol. 1978;96:109-36. doi: 10.1007/978-1-4757-0722-9_4.
The chick oviduct progesterone receptor has been purified to homogeneity by affinity chromatography and its molecular action studied in vitro. The native receptor is a 200,000 MW dimer of two dissimilar 4S subunits with different intranuclear function. The receptors directly regulate RNA chain initiation sites in oviduct chromatin by interactions involving target tissue nuclear acceptor sites. There is a 1:1 correspondence between receptor "acceptor" sites and RNA sites. Only the dimer form of the receptor is active in vitro on chromatin templates. The study suggests a novel model for hormone action which can be tested directly in this system.
通过亲和层析法已将鸡输卵管孕酮受体纯化至同质，并对其分子作用进行了体外研究。天然受体是由两个具有不同核内功能的不同4S亚基组成的200,000分子量的二聚体。这些受体通过涉及靶组织核受体位点的相互作用直接调节输卵管染色质中的RNA链起始位点。受体“受体”位点与RNA位点之间存在1:1对应关系。只有受体的二聚体形式在体外对染色质模板具有活性。该研究提出了一种激素作用的新模型，可在该系统中直接进行测试。
