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. 1976 Oct;73(10):3443–3447. doi: 10.1073/pnas.73.10.3443

ATP-PPi exchange activity of progesterone receptor.

V K Moudgil, D O Toft
PMCID: PMC431131  PMID: 185612

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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