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The Interaction of Thyroxine with Human Plasma Prealbumin and with the Prealbumin-Retinol-binding Protein Complex

From the ¹ From the Department of Medicine, Columbia University College of Physicians and Surgeons, New York, New York 10032

Prealbumin was isolated from human plasma by chromatography on columns of diethylaminoethyl Sephadex and Sephadex G-200, followed by preparative polyacrylamide gel electrophoresis. The prealbumin was homogeneous in the analytical ultracentrifuge with an s_20,w of 3.7 S and with a molecular weight of about 50,000. Prealbumin formed a protein-protein complex with plasma retinol-binding protein in a molar ratio of 1:1.

The interaction of thyroxine with prealbumin was quantitatively studied by the method of equilibrium dialysis with ¹³¹I-labeled thyroxine. Studies were conducted at 24° and at 37° in phosphate buffer, pH 7.4, and in phosphate buffer containing 0.14 m NaCl. Prealbumin was found to possess a single binding site for 1 molecule of thyroxine. The association constant for the thyroxine-prealbumin interaction was approximately 1.6 x 10⁷, and was only slightly affected by temperature change or by NaCl. The binding capacity and affinity of prealbumin for thyroxine were similar in the presence and absence of retinol-binding protein. Moreover, the binding of thyroxine to prealbumin did not interfere with the interaction of prealbumin with retinol-binding protein. The interaction of prealbumin with thyroxine appears to be independent of the prealbumin-retinol-binding protein interaction.

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