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Nucleic Acids Research, 1980, Vol. 8, No. 16 3535-3552
© 1980

MOLECULAR BIOLOGY

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

N.M. Kumar and I.O. Walker

Department of Biochemistry, University of Oxford South Parks Road, Oxford OX1 3QU, UK

Received July 14, 1980. 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°–37°C and independent of pH over the range 5.0 to 9.0. The curves are sigmoid, indicating co-operative disso ciation 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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