Skip to content
BY-NC-ND 3.0 license Open Access Published by De Gruyter June 2, 2014

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

  • Rüdiger Brust

Abstract

Rat liver chromatin has been fractionated by different solubility in solvents of 155 mᴍ 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.

Received: 1985-12-30
Revised: 1986-4-16
Published Online: 2014-6-2
Published in Print: 1986-10-1

© 1946 – 2014: Verlag der Zeitschrift für Naturforschung

This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 3.0 License.

Downloaded on 28.3.2024 from https://www.degruyter.com/document/doi/10.1515/znc-1986-9-1017/html
Scroll to top button