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. 1980 Aug 25;8(16):3535–3551. doi: 10.1093/nar/8.16.3535

The binding of histones H1 and H5 to chromatin in chicken erythrocyte nuclei.

N M Kumar, I O Walker
PMCID: PMC324173  PMID: 7433099

Abstract

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.

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Selected References

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