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A second human androgen receptor cDNA clone (hARb) encoding an identical amino terminal and DNA binding domains, but differing by four amino acids at the hormone binding domain, did not bind [3H]DHT with high affinity when incubated with protein expressed by in vitro transcription-translation. Co-transfection of hARa in an expression vector with mouse mammary tumor virus (MMTV)-bacterial chloramphenical acetyltransferase (CAT) chimeric plasmids, followed a hormone-dependent trans-activation, defining the binding affinity of hARa between 10^-9 M and 1 x 10^-8 M for [3H]DHT. A similar co-transfection experiment with hARb indicated a Kd of hARb for [3H]DHT to be above 10^-8 M. …
