Studies on Cellular Thyroxine-and Triiodothyronine-Binding Proteins
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چکیده
منابع مشابه
Effects of triiodothyronine and other thyroxine analogues on thyroxine-binding in human serum.
The strong affinity between thyroxine and the specific thyroxine-binding protein (TBP) of human serum (1) is apparent from, a) the inability to remove more than small amounts of thyroxine from the serum by prolonged dialysis (2), and b) the effectiveness with which TBP competes with albumin for available thyroxine in serum, despite its much smaller concentration. Thyroxine bound to TBP is, neve...
متن کاملThyroxine-protein interactions. Interaction of thyroxine and triiodothyronine with human thyroxine-binding globulin.
The effect of temperature on the binding of thyroxine and triiodothyronine to thyroxine-binding globulin has been studied by equilibrium dialysis. Inclusion of ovalbumin in the dialysis mixture stabilized thyroxine-binding globulin against losses in binding activity which had been found to occur during equilibrium dialysis. Ovalbumin by itself bound the thyroid hormones very weakly and its bind...
متن کاملSalicylate-induced increases in free triiodothyronine in human serum. Evidence of inhibition of triiodothyronine binding to thyroxine-binding globulin and thyroxine-binding prealbumin.
Addition of sodium salicylate to human serum at concentrations often obtained during aspirin therapy causes 100-200% increases in free triiodothyronine (T(3)) and free thyroxine (T(4)) as estimated by ultrafiltration. The increase in free T(3) was unexpected since previous data had suggested that salicylate inhibits binding of T(4) only to thyroxine-binding prealbumin (TBPA) and that T(3) is no...
متن کاملStudies on Human Thyroxine - Binding Globulin
to large volumes of serum may be due to adsorption of neuraminidases to the Sepharose either directly from serum or as the result of bacterial contamination. Partial desialylation of TBG in vivo may be an early step in the catabolism of this protein.
متن کاملPhysiological and pharmacological influences on thyroxine to 3,5,3'-triiodothyronine conversion and nuclear 3,5,3'-triiodothyronine binding in rat anterior pituitary.
Our recent in vivo studies have suggested that intrapituitary l-thyroxine (T(4)) to 3,5,3'-triiodo-l-thyronine (T(3)) conversion with subsequent nuclear binding of T(3) is an important pathway by which circulating T(4) can inhibit thyrotropin release. The present studies were performed to evaluate various physiological and pharmacological influences on these two processes in rat anterior pituit...
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ژورنال
عنوان ژورنال: Folia Endocrinologica Japonica
سال: 1966
ISSN: 0029-0661
DOI: 10.1507/endocrine1927.41.10_1191