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An aqueous two-phase partitioning study of partially purified nuclear thyroid hormone receptor from rat liver was performed. Stability of 3,5,3'-tri-iodo-L-thyronine (T₃)–receptor complex and T₃-binding activity in the presence of dextran or polyethylene glycol were assessed in order to determine the amount of occupied or unoccupied receptors in each phase. Partition coefficients were calculated as the ratio of receptor concentration in the upper polyethylene glycol-rich phase H₂O and that in the lower dextranrich phase H₂O. The partition coefficient was a sensitive function of the salt at pH above 6·1 and below 5·1. The salt had no effect on the partition coefficient at pH around 5·6. These results suggest that the isoelectric point of the thyroid hormone receptor is about 5·6, confirming previous determinations using isoelectric focusing. The partition coefficient of the receptor decreased upon T₃ binding, regardless of the salt composition. In contrast, the partition coefficient of thyroxine-binding globulin increased upon T₃ binding. Free T₃ preferentially partitioned into the upper polyethylene glycol-rich phase and gave a partition coefficient higher than 1·0. These results strongly suggest that the decrease in the partition coefficient of the receptor upon hormone binding reflects conformational changes or changes in electrostatic properties of the receptor upon hormone binding. Such an alteration may be involved in biological activation of the receptor upon hormone binding.

J. Endocr. (1988) 119, 431–437

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				T. Kakizawa, T. Miyamoto, A. Kaneko, H. Yajima, K. Ichikawa, and K. Hashizume Ligand-dependent Heterodimerization of Thyroid Hormone Receptor and Retinoid X Receptor J. Biol. Chem., September 19, 1997; 272(38): 23799 - 23804. [Abstract] [Full Text] [PDF]