title: Soluble and insoluble rat liver chromatin is different in structure and protein composition.
abstract: Rat liver chromatin has been fractionated by different solubility in solvents of 155 mM ionic strength in soluble S and insoluble I-chromatin. Histone H1 content is lower in S as compared to I-chromatin. The HMG1/2 nonhistone proteins are observed in S-chromatin and in the nuclear pelleted residue from the chromatin isolation procedure, but no amount can be detected in I-chromatin. Thermal denaturation profiles and CD-spectra are different for S and I-chromatin indicating distinct interactions between DNA and proteins in the chromatin molecules. Both effects, differing protein content and distinct DNA-protein interactions, can be correlated with solubility and insolubility being the result of charge-charge interactions between chromatin molecules and ionic components of the solvent.
mesh_terms: D000818:Animals; D002458:Cell Fractionation / Q000379:methods; D002843:Chromatin / Q000302:isolation & purification* / Q000648:ultrastructure; D002942:Circular Dichroism; D004247:DNA / Q000302:isolation & purification; D006609:High Mobility Group Proteins / Q000032:analysis; D006657:Histones / Q000032:analysis; D008099:Liver / Q000648:ultrastructure*; D009691:Nucleic Acid Denaturation; D009698:Nucleoproteins / Q000032:analysis*; D051381:Rats; D012995:Solubility
chemical_list: D002843:Chromatin; D006609:High Mobility Group Proteins; D006657:Histones; D009698:Nucleoproteins; D004247:DNA