Abstract
When H3-progesterone is incubated with chick oviduct cytosol, it binds to a specific receptor protein. The subsequent binding of this complex to oviduct chromatin is greater than that of free progesterone alone. This specific affinity for the progesterone-receptor complex is not observed with spleen, heart, liver or erythrocyte chromatin. Progesterone incubated with the cytosols of non-target tissues such as liver or spleen shows no specific binding to chromatin from any source. Artificial complexes of chick histone and DNA display a low degree of non-specific binding. The results suggest that the chromatin of target tissue (oviduct) may contain "acceptor" sites for the hormone-receptor complex contained in the cytoplasm of the cell. The genome may thus be preprogrammed to receive the hormone receptor complex as it enters the nucleus of the target cell.
Original language | English (US) |
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Pages (from-to) | 20-27 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 43 |
Issue number | 1 |
DOIs | |
State | Published - Apr 2 1971 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology