The binding of histones H1 and H5 to chromatin in chicken erythrocyte nuclei.
The binding curves of histones H1 and H5 to chromatin in nuclei have been determined by a novel method which utilises the differential properties of free and bound histones on cross-linking with formaldehyde. The dissociation is thermodynamically reversible as a function of [NaCl]. The binding curves are independent of temperature over the range 4 degrees - 37 degrees C and independent of pH over the range 5.0 to 9.0. The curves are sigmoid, indicating co-operative dissociation with NaCl. The standard free energy of dissociation in 1 M NaCl for H1 is 0.5 Kcals/mole and for H5 is 3.5 Kcals/mole.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002645:Chickens; D002843:Chromatin / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006657:Histones / Q000097:blood*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009994:Osmolar Concentration; D013816:Thermodynamics
D002843:Chromatin; D006657:Histones