Reactivation of affinity-purified estrogen receptors by peptides derived from histone H2B

Purification of estrogen receptors by affinity chromatography over diethylstilbestrol-agarose is associated with a major loss of estradiol binding activity. Histone H2B can restore a significant fraction of the binding activity. Cleavage of the H2B molecule into two halves by cyanogen bromide reveals that the carboxyl terminus is responsible for the major reactivating effects.