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.
McArdle Laboratory for Cancer Research, The University of Wisconsin-Madison 53706.
K K
KK
Bhattacharyya
M R
MR
Olsen
G C
GC
Mueller
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