Analysis of estrogen and antiestrogen receptor complexes
The author used affinity labeling ligands for the estrogen receptor (ER) to examine the structure and relatedness of ER in different target tissues and species. In addition, he characterized the first efficient and selective affinity labeling estrogen, ketononestrol aziridine (KNA). KNA has an apparent relative binding affinity of 8% that of estradiol and shows time-dependent irreversible binding to the ER. The agonistic activity of KNA is evident in MCF-7 cells in culture, where it increases cell growth rate and elevates the level of progesterone receptor. Labeling with (/sup 3/H)KNA proceeds in a time-, concentration-, and temperature-dependent manner; labeling is efficient and selective and, by competition studies, was shown to be estrogen specific. ER covalently labeled with (/sup 3/H)KNA sediments as a 4S species on high salt sucrose gradients, and its sedimentation position is shifted by treatment with monoclonal antibodies. On SDS-polyacrylamide gels, the labeled species migrates with a molecular weight (M/sub r/) of 66,000 daltons.
- Research Organization:
- Illinois Univ., Urbana (USA)
- OSTI ID:
- 6292436
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
BIOCHEMICAL REACTION KINETICS
CHEMICAL COMPOSITION
COMPLEXES
DOSE-RESPONSE RELATIONSHIPS
ELECTROPHORESIS
ESTROGENS
HORMONES
ISOTOPE APPLICATIONS
KINETICS
LABELLED COMPOUNDS
LABELLING
MEMBRANE PROTEINS
MOLECULAR STRUCTURE
MOLECULAR WEIGHT
ORGANIC COMPOUNDS
PROTEINS
REACTION KINETICS
RECEPTORS
STEROID HORMONES
TEMPERATURE DEPENDENCE
TIME DEPENDENCE
TRACER TECHNIQUES
TRITIUM COMPOUNDS