title: [Is the binding strength of histone fractions with DNA different?].
abstract: The dissociation of histones H1, H2B and H2A from DNA was shown for the first time in the medium of physiological ionic strength (0.15M NaCl + 0.7 mM Na-phosphate buffer, pH 7.0) by treating the whole histone--DNA complex with high concentrations of whole histone from calf thymus chromatin. The histones can be separated into three groups according to the strength of their binding to DNA: H1 < H2B + H2A < H3 + H4. It is suggested that histone octamer is not a conservative formation and the histone content of nucleosomes may change under physiological conditions being affected by competition of chromatin components for DNA.
mesh_terms: D000818:Animals; D002417:Cattle; D002843:Chromatin / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D066298:In Vitro Techniques; D009698:Nucleoproteins / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism; D011485:Protein Binding / Q000187:drug effects; D013950:Thymus Gland / Q000378:metabolism
chemical_list: D002843:Chromatin; D006657:Histones; D009698:Nucleoproteins; D009707:Nucleosomes; D004247:DNA
vernacular_title: Razlichna li prochnost' sviazi gistonovykh fraktsiĭ s DNK?