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Development of DHT-receptor (DHT-R) estimation through (3H)-DHT exchange

The convenient dihydrotestosterone-(DHT)-R estimation with (3H)-methyltrienolone (R1881)in human tissue is unspecific as it is also bound by the progestin receptors. We have, therefore, developed a highly specific (3H)-DHT exchange assay for cytoplasmic and nuclear DHT-R. In parallel to the suppression of DHT metabolism during incubation by NADase, suppression of low capacity binding was carried out in the presence of an overdose (100-fold) of R1881. In this way, the residual metabolism of (3H)-DHT remained equal in both assays. Free (3H)-DHT and sex hormone binding globulin (SHBG) were separated by agar gel electrophoresis (R. Wagner, 1972). Under these conditions, the binding characteristics of DHT and R1881 were not different in relation to KS value (5.08×10-9 mol/1), association and dissociation velocities, and number of estimated binding sites (free 0.5 fmol/mgDNA; total 1.C fmol/mg DNA). The data indicate that the higher affinity of R1881 to the DHT-R may not be real as DHT concentration diminishes in the usual assay systems.