Abstract

Various histone fractions from several sources differ markedly in their degree of dependence on protein kinase stimulatory modulator for maximum phosphorylation by rat liver cyclic GMP-dependent protein kinase in the presence of cyclic GMP. DEAE-cellulose and QAE-Sephadex chromatography of arginine-rich and mixed histones resulted in the histones displaying increased dependence on the modulator. This increased dependence was apparently due to the removal of contaminating modulator as heat-stable modulator activity could be eluted from the DEAE-cellulose column. Lysine-rich histone was not markedly dependent on the modulator before or after QAE-Sephadex chromatography.

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