Histone binding to isolated rat liver nuclei.
Calf thymus histone H3 bound irreversibly to the isolated rat liver nuclei. The rate and extent of binding was a function of the incubation period and the concentration of both H3 and nuclei, but independent of the temperature. The binding was saturable and was inhibited by simultaneous presence of various histones. Approximately 94% of the bound H3 was associated with nuclear membrane fraction.
D000818:Animals; D002250:Carbon Radioisotopes; D002417:Cattle; D002458:Cell Fractionation; D002467:Cell Nucleus / Q000378:metabolism* / Q000648:ultrastructure; D005557:Formaldehyde / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats
D002250:Carbon Radioisotopes; D006657:Histones; D005557:Formaldehyde