Binding of estradiol receptor complexes to isolated human breast chromatin

The interaction of estradiol-receptor complexes and isolated human breast tumor chromatin was studied under equilibrium conditions. The estradiol-receptor complexes bound specifically to the chromatin of hormone dependent tumors and showed a single class of binding sites with a Ka of 0.96 × 1010m-1...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Charreau, E.H., Baldi, A.
Formato: JOUR
Materias:
dna
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03008177_v16_n2-3_p79_Charreau
Aporte de:
Descripción
Sumario:The interaction of estradiol-receptor complexes and isolated human breast tumor chromatin was studied under equilibrium conditions. The estradiol-receptor complexes bound specifically to the chromatin of hormone dependent tumors and showed a single class of binding sites with a Ka of 0.96 × 1010m-1 and a binding capacity of 1.5 pmoles/mg DNA. The binding was a temperature-dependent process and involved a "transformation" of the receptor protein. The heat-activated hormone-receptor com-plex was more active than the 8S form in the binding phenomenon. The specific interaction of estradiol-receptor complex with isolated chromatin was saturable and sensitive to conditions of temperature and ionic strength. Furthermore under optimal conditions no acceptor sites were detected in chromatin of hormone independent tumors. © 1977 Dr. W. Junk b.v. Publishers.