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We investigated the effects of medical, industrial and agricultural chemicals on 3,3′,5-L-[ 125 I]triiodothyronine ([ 125 I]T 3 ) binding to purified recombinant  Xenopus laevis  ( X. laevis ) transthyretin (xTTR), a plasma thyroid hormone-binding protein, and to the ligand-binding domain of thyroid hormone receptor-β (xTR LBD). xTTR derived from  X. laevis  serum had about 80 times higher affinity for T 3  than for L-thyroxine. The xTTR's relative affinities for diethylstilbestrol, pentachlorophenol and ioxynil were 10 −1 - to 10 −2 -fold less than that for T 3 . However, all chemicals investigated had either a weak or no influence on [ 125 I]T 3  binding to xTR LBD. The concentration of diethylstilbestrol, the most potent chemical, required for 50% inhibition of [ 125 I]T 3  binding to xTR LBD was 10 4  times greater than that of unlabeled T 3 . These results indicate the existence of several chemicals that interact with xTTR but not with xTR LBD.

The Effects of Endocrine-Disrupting Chemicals on Thyroid Hormone Binding to Xenopus laevis Transthyretin and Thyroid Hormone Receptor