3'-Monoiodothyronine degradation in rat liver homogenate: enzyme characteristics and documentation of deiodination by high-pressure liquid chromatography.

Characteristics of 3'-monoiodothyronine (3'-T1) degradation were examined in vitro in rat tissue homogenates. In rat liver homogenates, 3'-T1 degradation was optimal at pH 7.4, and was dependent upon time, temperature, and tissue concentration. The Michaeli's constant (Km) = 0.84 mumol/L. 3'-T1 degradation was enhanced by dithiothreitol and inhibited by propylthiouracil, sodium ipodate, ANS, and sodium azide but not by methimazole. Animals that fasted for three days had significant reductions in both hepatic T4 to T3 conversion (199 +/- 12 v 116 +/- 12 pg T3 generated/mg protein; P less than 0.001) and 3'-T1 degradation (588 +/- 31 v 148 +/- 53 pg 3'-T1 degraded/mg protein; P less than 0.001). To document that 3'-T1 degradation was occurring by deiodination, both liver and kidney homogenates were incubated with 125I-3'-T1 (approximately 3 microCi; 13.1 nmol/L). The reaction products were separated on a reverse-phase high pressure liquid chromatography (HPLC) column. In both tissues an iodide peak was generated, and no other radiolabeled peaks appeared except for 125I-3'-T1. These data suggest that 3'-T1 is metabolized by phenolic-ring monodeiodination and is enzymic in nature.