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• W1994410081 abstract "Abstract The androgen-receptor complexes in the ventral prostate cytosol fraction are found in different molecular forms, depending on the experimental conditions. By gel fitration two different complexes are found. One is excluded and the other is retained on a column of Sephadex G-100. By experiments in vivo a 6–6.5 S androgen-receptor complex is observed on sucrose gradients. This complex dissociates into a 3.5–4 S complex after dialysis against 0.5 M NaCl (in buffer) for 20 h. The androgen-binding proteins extracted from the nuclear pellet with 0.5 M NaCl move as a sharp peak on sucrose gradients, with a sedimentation constant of 3 S. The epididymis of adult castrated rats also contains similar proteins, which bind 5α-dihydrotestosterone (5α-DHT) with high affinity and low capacity. The 5α-DHT binding protein in the cytosol fraction of epididymal homogenates is slightly retained on a column of Sephadex G-100, and moves with a sedimentation rate of about 4–4.5 S (mean 4.3 S) on sucrose gradients. Similar results are obtained both at high and low ion strength. The binding of [3H]5α-DHT to this protein is easily depressed by small amounts of non-labelled 5α-DHT. 15 min after the injection of [3H]testosterone in vivo. about 90% of the radioactivity bound to proteins moves as 5α-DHT on t.l.c. 1 h alter the injection of 60 μCi[3H]5α-DHT in vivo, a considerable part of the radioactivity is found in the nuclear fraction of homogenized epididymal tissue. Human hyperplastic prostatic tissue also contains similar androgen-binding proteins. The binding of androgens to these macromolecules is inhibited by potent anti-androgenic compounds such as SK & F 7690 and cyproterone. Some evidence for direct binding of [3H]cyproterone-acetate in the ventral prostate cytosol fraction is presented." @default.
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• W1994410081 date "1972-04-01" @default.
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• W1994410081 title "Studies on the interaction between androgen and macromolecules in male accessory sex organs of rat and man" @default.
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• W1994410081 doi "https://doi.org/10.1016/0022-4731(72)90089-1" @default.
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