Abstract
The binding of rat liver nuclear non-histone proteins to DNA has been detected using a membrane filter technique. Binding is optimal at 0.05 M NaCl, increases with decreasing pH, and is enhanced in the presence of Mg 2+. About 50% of the DNA is bound reversibly. Histone contamination of non-histone preparations contributes little, if at all, to the observed binding while cytoplasmic proteins, isolated like non-histones, have no ability to bind DNA. The binding activity, which is unstable, can be destroyed by heat or pronase.
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