Rat alpha-fetoprotein-estrogen interaction

Rat alpha-fetoprotein-estrogen interaction

The influence of temperature, pH, ionic strength and sulphydryl reagents on the binding of estrogen to alpha-fetoprotein was studied. Equilibrium dialysis experiments showed that under optimal conditions, the association constant is high (Ka = 3 × 108M−1) and one binding site per alpha-fetoprotein m...

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Veröffentlicht in:Journal of steroid biochemistry 1978-06, Vol.9 (6), p.547-551
Hauptverfasser: Aussel, Claude, Masseyeff, René
Format: Artikel
Sprache:eng
Schlagworte:
alpha-Fetoproteins - metabolism
Androgens - pharmacology
Animals
Binding Sites
Chloromercuribenzoates - pharmacology
Estradiol - metabolism
Estrogens - metabolism
Estrone - metabolism
Hydrogen-Ion Concentration
Osmolar Concentration
Protein Binding
Rats
Thermodynamics
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Zusammenfassung:The influence of temperature, pH, ionic strength and sulphydryl reagents on the binding of estrogen to alpha-fetoprotein was studied. Equilibrium dialysis experiments showed that under optimal conditions, the association constant is high (Ka = 3 × 108M−1) and one binding site per alpha-fetoprotein molecule was demonstrated. This binding was shown to be specific for estrone and estradiol. Anti-estrogenic compounds are not bound by alpha-fetoprotein. Rat alpha-fetoprotein appears to differ by several functional differences from uterine estrogen receptors.
ISSN:0022-4731
DOI:10.1016/0022-4731(78)90121-8