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As a model for the nonspecific interaction of steroid receptors with DNA, the binding of estradiol.receptor complexes of mouse kidney and uterine cytosols to oligo(dT)-cellulose was studied in detail. A limited concentration range of monovalent cationic salts was required for optimal binding, regardless of prior activation of the receptor complexes or the oligomer ligand. Thermal activation of the receptor complexes did not facilitate binding. The reaction was selective for intracellular steroid hormone.receptor complexes, as extracellular proteins binding estradiol with low affinity (bovine serum albumin) or high affinity (mouse alpha-fetoprotein) were inactive. Both crude and partially purified kidney cytosol receptor complexes bound preferentially to oligo(dT)- and oligo(dC)-celluloses, rather than oligo(dA)-celluloses. These findings suggest that at least part of the nonspecific interaction of estradiol.receptor complexes with native DNA is through a salt-sensitive binding of the complex to pyrimidine-rich surfaces of the DNA.
K H Thanki, and
T A Beach, and
H W Dickerman
June 1982,
British journal of cancer,
K H Thanki, and
T A Beach, and
H W Dickerman
July 1979,
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K H Thanki, and
T A Beach, and
H W Dickerman
February 1975,
Cell,
K H Thanki, and
T A Beach, and
H W Dickerman
June 2006,
CSH protocols,
K H Thanki, and
T A Beach, and
H W Dickerman
January 1976,
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K H Thanki, and
T A Beach, and
H W Dickerman
June 1989,
The EMBO journal,
K H Thanki, and
T A Beach, and
H W Dickerman
July 1974,
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K H Thanki, and
T A Beach, and
H W Dickerman
December 1975,
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K H Thanki, and
T A Beach, and
H W Dickerman
January 2000,
Bioconjugate chemistry,
K H Thanki, and
T A Beach, and
H W Dickerman
May 1976,
Analytical biochemistry,
