ATP-PPi exchange activity of progesterone receptor.
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.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D011756:Diphosphates / Q000378:metabolism*; D005260:Female; D008345:Manganese / Q000494:pharmacology; D010057:Oviducts; D010618:Phenanthrolines / Q000494:pharmacology; D011980:Receptors, Progesterone / Q000032:analysis / Q000187:drug effects / Q000378:metabolism*; D012294:Rifamycins / Q000494:pharmacology
D011756:Diphosphates; D010618:Phenanthrolines; D011980:Receptors, Progesterone; D012294:Rifamycins; D008345:Manganese; D000255:Adenosine Triphosphate