Effect of aggregation of histone octamers in high-salt solutions on circular dichroism spectra

The circular dichroism (CD) of freshly prepared chicken erythrocyte core histones has been reexamined in high concentrations of ammonium sulfate and sodium chloride, conditions which cause drastic changes in the solubility and aggregative properties of these proteins. After sample clarification by ultracentrifugation, no significant net changes are detected in the secondary structure of the core histones in the range of 2.0-2.5 M ammonium sulfate. There is also no significant difference between the CD spectra of histone solutions in 2 M sodium chloride and clarified solutions of histones in high concentrations of ammonium sulfate. It was observed that sample clarification by ultracentrifugation immediately prior to taking CD spectra was necessary for signal stabilization, especially under conditions which begin to favor crystallization of the histones.