Abstract
Intravenous infusion of labeled T3 to adult dogs followed by analysis of gradient-dialyzed 0.4 m KCl extracts of chromatin from nuclei of cerebral cortex gave in vivo evidence of soluble chromatin-associated thyroid hormone-binding proteins. Subsequent in vitro Sepharose 4B column chromatography of soluble brain chromatin extract and cytosol proteins provided evidence of specific binding of both labeled T3 and T4. Kinetic analysis of in vitro T3 and T4 binding to chromatin extract and to a Sepharose-purified cytosol fraction showed specific binding in each which appeared of low-affinity, high-capacity type. It is suggested that the soluble-binding activity demonstrated may be characterized as a relatively large, slowly equilibrating pool of intracellular thyroid hormone-binding protein.
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