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Journal of Andrology, Vol 4, Issue 4 248-252, Copyright © 1983 by The American Society of Andrology
JOURNAL ARTICLE |
S. Gulizia, R. D'Agata, B. M. Sanborn and E. Steinberger
Leydig cells, purified on two sequential Percoll gradients to purities of 89 +/- 1%, were used to study the binding of 17-beta-hydroxy-17 alpha-methyl-estra-4,9,11-triene-3-one(3H-R1881). The accumulation of 3H-R1881 in the nuclear fraction of these cells was time- and temperature-dependent. Specific binding was saturable with an apparent Ka of 0.14 nM-1 and a single class of binding sites at a concentration of 721 fmol/mg DNA. A fraction of the bound radioactivity in the nuclear pellet could be extracted with 0.4 M KCl, and a portion of this extracted steroid was associated with macromolecular species. The nuclear accumulation was androgen-specific. These data are consistent with the presence of androgen receptors in rat Leydig cells.
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