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Binding of 3H‐Methyltrienolone (3H‐R1881) to cytoplasmic androgen receptor protein and its translocation into nuclei in human gingiva was demonstrated. 3H‐R1881 binds to androgen receptors with high affinity (Kd= 1.7−1.9 × 10−9 M) and low capacity (10–16 fmol/mg protein). The binding was specific for DHT binding sites and was destroyed by proteolytic enzymes (pronase and trypsin). These results suggest that 3H‐R1881 can be used as a ligand in combination with nonradioactive DHT to study androgen receptors in the gingiva.
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Vittek et al. (1985) studied this question.
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