Abstract
The initial velocity kinetics of the effect of thyroid hormone and analogs on human placental microsomal aromatase were studied. Thyroxine and its propionic analog 3,5,3',5'-tetraiodothyropropionic acid show a competitive inhibition with an apparent Ki of 1.4 microM and 8.5 microM, respectively, towards androstenedione aromatization. 3,5,3'-Triiodothyronine with a Ki of 1.8 microM shows a decreased affinity compared to thyroxine. Two analogs, 3,5,3'-triiodothyropropionic acid and 3,5,3'-triiodothyroacetic acid appear to have negligible competition.
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