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Am J Physiol 200: 1029-1031, 1961;
0002-9513/61 $5.00
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Uptake and binding of thyroxine and triiodothyronine by rat diaphragm in vitro

Allen Lein 1 and Robert M. Dowben 1

1 Departments of Physiology and Medicine, Northwestern University, Chicago, Illinois

Hemidiaphragms from weanling Sprague-Dawley rats were incubated in Krebs-Ringer buffer containing 1.3 x 10–7 m l-thyroxine or l-triiodothyronine labeled with radioiodine. Triiodothyronine uptake was about twice as rapid as thyroxine uptake. The data were consistent with a kinetic analysis based on a two-step process: 1) simple diffusion into the tissue (rate-limiting step) and 2) binding to cellular proteins (a process that occurs very rapidly compared to diffusion). The diffusion constants were calculated to be kd(T4) = 0.153 cm3/min and kd(T3) = 0.352 cm3/min. The data suggest a single species of tissue-binding site with identical tissue-binding capacity and binding affinity for both triiodothyronine and thyroxine. Maximum binding was found to be 28 x 10–4 µm/g tissue and the affinity constant for binding was 1.4 x 104 g/µm. The difference in the rate of accumulation of thyroxine and triiodothyronine appears to be due only to the difference in the diffusion rate. A direct rate equation for the accumulation of thyroid hormone was derived. Points calculated by means of this equation fit remarkably well with the experimental data.

Submitted on November 10, 1960




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Plasma Membrane Transport of Thyroid Hormones and Its Role in Thyroid Hormone Metabolism and Bioavailability
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[Abstract] [Full Text] [PDF]




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