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.
Bhattacharyya
K K
KK
McArdle Laboratory for Cancer Research, The University of Wisconsin-Madison 53706.
Olsen
M R
MR
Mueller
G C
GC
D000818:Animals; D002846:Chromatography, Affinity; D004958:Estradiol / Q000378:metabolism; D005260:Female; D006657:Histones / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology*; D011817:Rabbits; D011960:Receptors, Estrogen / Q000187:drug effects* / Q000302:isolation & purification / Q000378:metabolism
D006657:Histones; D010446:Peptide Fragments; D011960:Receptors, Estrogen; D004958:Estradiol