Dihydrotestosterone receptors in the human prostate: characterization by chromatography, electrophoresis, and...

The human prostate androgen receptor was characterized by Sephadex G-100 chromatography, acrylamide-DATD gel electrophoresis, and isoelectric focusing. A KCl nuclear extract was prepared and incubated in the presence of tritiated DHT or R1881 at 4 degrees C for 18 h. In the absence of proteolytic enzyme inhibitors, a fraction of the hormone receptor complex was excluded from the G-100 column, whereas another fraction migrated with proteins having apparent molecular weights in the area of 34,000 daltons. The complex migrated on gel electrophoresis only after mild trypsinization. As for the isoelectric focusing, the nuclear complex showed two forms specifically bound to [3H]androgens with pI in the area of 4.7 and 7.9, respectively.