High affinity thyroid hormone binding sites on purified rat liver plasma membranes. |
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Authors: | N B Pliam I D Goldfine |
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Affiliation: | Department of Medicine, Veterans Administration Hospital and the University of California, San Francisco, California USA |
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Abstract: | Two orders of saturable binding sites for L-T3 were detected on purified rat liver plasma membranes--a high affinity, low capacity binding site with a Kd of 3.2 ± 0.5 nM, and a lower affinity, higher capacity site with a Kd of 220 ± 50 nM. Competition-inhibition studies revealed that both D-T3 and L-T4 (two compounds with lower biological potencies than L-T3) were also less potent than L-T3 in competing for these binding sites. The present studies demonstrate, therefore, the presence of specific thyroid hormone binding sites on rat liver plasma membranes. In addition, they suggest that these sites may have a role both in mediating the known effects of thyroid hormones on membrane functions, and in regulating the entry of thyroid hormones into target cells. |
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Keywords: | Reprint address: Veterans Administration Hospital Endocrinology-Metabolism Section (111F) 4150 Clement Street San Francisco California 94121. |
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