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- W291341804 abstract "The relative competitive activity of a number of androstane derivatives was determined according to the 50% displacement of (/sup 3/H) estradiol from complexes with an unusual estrogen-binding protein (UEBP) of the liver of male rats. It was shown that: (1) the bulk of the energy of the bond of the steroid to protein is due to hydrophobic interactions; (2) the real ability to form specific complexes with the UEBP at androgen concentrations close to the physiological is determined by the 17..beta..-hydroxyl and is enhanced by the 3..cap alpha..- or 2..cap alpha..-hydroxy group; (3) the 3- and 17-keto groups weaken the interaction of androgens with the UEBP; (4) cis-coupling of the A and B rings in the molecule of androgens does not prevent the binding of the steroids to protein. These data substantially refine the concepts of the mechanisms of the interaction of androgens with the UEBP and may promote an elucidation of the physiological function of this protein." @default.
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- W291341804 date "1986-11-10" @default.
- W291341804 modified "2023-09-27" @default.
- W291341804 title "Unusual estrogen-binding liver protein: additional data on the structural determinants of androgenic ligands" @default.
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