Moudgil V K, Toft D O
Proc Natl Acad Sci U S A. 1976 Oct;73(10):3443-7. doi: 10.1073/pnas.73.10.3443.
Progesterone receptor preparations from avian oviduct catalyze a pyrophosphate (PPi)-exchange reaction between ATP and 32P-labeled PPi. The reaction requires ATP exclusively and is Mn++-dependent. This enzyme activity is detectable in receptor preparations that have been purified extensively by chromatography on ATP-Sepharose and DEAE-Sephadex columns. Polyacrylamide gel electrophoresis of purified preparations reveals a comigration of [3H]progesterone-receptor complex and the enzyme activity. The PPi-exchange reaction is inhibited by both o-phenanthroline and rifamycin AF/013, which also block the nuclear binding of progesterone receptor. These findings indicate that progesterone receptor may be an enzyme or a subunit of an enzyme that is active in nucleotide metabolism.
来自禽输卵管的孕酮受体制剂催化ATP与32P标记的焦磷酸（PPi）之间的焦磷酸交换反应。该反应仅需要ATP，且依赖于Mn++。这种酶活性在通过ATP-琼脂糖和DEAE-葡聚糖凝胶柱进行广泛色谱纯化的受体制剂中可检测到。纯化制剂的聚丙烯酰胺凝胶电泳显示[3H]孕酮受体复合物与酶活性共同迁移。邻菲罗啉和利福霉素AF/013均抑制PPi交换反应，它们也会阻断孕酮受体的核结合。这些发现表明孕酮受体可能是一种在核苷酸代谢中具有活性的酶或酶的亚基。
