Rachev R R, Dimitrov M I, Filipova E Kh, Dimitrov O A, Gaĭdarova K D
Probl Endokrinol (Mosk). 1979 Nov-Dec;25(6):60-5.
The binding of I125-triiodothyronine by male thyroidectomized rat liver nuclei and mitochondria in vivo and in vitro was studied. Labeled triiodothyronine was bound by the liver nuclei and mitochondria proteins. 90% radioactivity was bound by the nuclear nonhistone proteins. The binding of I125-triiodothyronine to the nuclei and mitochondria protein receptors was inhibited by unlabeled triiodothyronine and ICl. It is suggested that aromatic amino acids serve as the binding sites of the protein receptors, and that iodine atoms in the thyroid hormone molecules participated directly in the binding process.
研究了雄性甲状腺切除大鼠肝脏细胞核和线粒体在体内和体外对I125 - 三碘甲状腺原氨酸的结合情况。标记的三碘甲状腺原氨酸与肝脏细胞核和线粒体蛋白质结合。90%的放射性与核非组蛋白结合。未标记的三碘甲状腺原氨酸和ICl可抑制I125 - 三碘甲状腺原氨酸与细胞核和线粒体蛋白质受体的结合。提示芳香族氨基酸作为蛋白质受体的结合位点，且甲状腺激素分子中的碘原子直接参与结合过程。
