Soluble and Insoluble Rat Liver Chromatin is Different in Structure and Protein Composition

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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.