Two high-affinity ligand binding states of uterine estrogen receptor distinguished by modulation of hydrophobic environment

The steroid binding function of soluble (cytosolic) estrogen receptors from calf uteri was evaluated under conditions known to modify the extent of hydrophobic interaction with receptor-associated proteins. Receptor preparations were equilibrated into 6 M urea (+/- 0.4 M KCl) buffers and control buf...

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Veröffentlicht in:	Biochemistry (Easton) 1987-02, Vol.26 (3), p.722-727
Hauptverfasser:	Hutchens, T. William, Li, Chee Ming, Zamah, Nezaam M, Besch, Paige K
Format:	Artikel
Sprache:	eng
Schlagworte:	550601 - Medicine- Unsealed Radionuclides in Diagnostics ANIMALS Biological and medical sciences BODY Buffers CALVES CATTLE Cell receptors Cell structures and functions CHROMATOGRAPHY CONFIGURATION INTERACTION Cytosol - metabolism DOMESTIC ANIMALS ESTRADIOL Estradiol - metabolism ESTRANES ESTROGENS Female FEMALE GENITALS Fundamental and applied biological sciences. Psychology HORMONES HYDROXY COMPOUNDS ION EXCHANGE ISOTOPE APPLICATIONS Kinetics LABELLED COMPOUNDS LIGANDS MAMMALS MEMBRANE PROTEINS Molecular and cellular biology ORGANIC COMPOUNDS ORGANS PROTEINS RADIOLOGY AND NUCLEAR MEDICINE RADIORECEPTOR ASSAY RECEPTORS Receptors, Estrogen - metabolism RUMINANTS SEPARATION PROCESSES STEROID HORMONES STEROIDS TRACER TECHNIQUES TRITIUM COMPOUNDS Urea - pharmacology UTERUS Uterus - metabolism VERTEBRATES
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