Effect of long-chain fatty acids on the binding of thyroxine and triiodothyronine to human thyroxine-binding globulin
| Autor: | Ladislav Korcek, Milton Tabachnick |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
medicine.medical_specialty
Linolenic Acids Globulin Linoleic acid Palmitic Acid Biophysics Oleic Acids Palmitic Acids Biochemistry Linoleic Acid Palmitic acid Structure-Activity Relationship Thyroxine-Binding Proteins chemistry.chemical_compound Thyroxine-binding globulin Internal medicine medicine Humans Molecular Biology chemistry.chemical_classification Triiodothyronine Chromatography biology alpha-Linolenic acid Fatty Acids alpha-Linolenic Acid Fatty acid Molecular Weight Kinetics Thyroxine Oleic acid Endocrinology Linoleic Acids chemistry biology.protein Stearic Acids Oleic Acid |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 881:292-296 |
| ISSN: | 0304-4165 |
| DOI: | 10.1016/0304-4165(86)90016-4 |
| Popis: | The effect of long-chain fatty acids on the binding of thyroxine to highly purified human thyroxine-binding globulin has been studied by equilibrium dialysis performed at pH 7.4 and 37 degrees C. At a fixed molar ratio of 2000:1 of fatty acid to thyroxine-binding globulin, the degree of binding inhibition based on the percent change in nK value relative to the control as determined from Scatchard plots was: palmitic, 0%; stearic, 0%; oleic, 76%; linoleic, 69%; and linolenic, 61%. At a 500:1 molar ratio of oleic acid to thyroxine-binding globulin, equivalent to 0.125 mM free fatty acid in serum, thyroxine binding was inhibited by 18%, increasing to 93% at a 4500:1 molar ratio. At molar ratios of oleic acid to thyroxine-binding globulin of 1000:1, 2000:1 and 4000:1, the degree of inhibition of triiodothyronine binding was 24%, 41% and 76%, respectively. The results indicate that the unsaturated long-chain fatty acids are potent inhibitors of thyroxine binding to thyroxine-binding globulin, whereas the saturated fatty acids have little or no effect on thyroxine binding. |
| Databáze: | OpenAIRE |
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