PMID: 6406109Jan 1, 1983Paper

Hyperthyroxinaemia: abnormal binding of T4 by an inherited albumin variant

Clinical Endocrinology
M R LallozR L Himsworth

Abstract

Two euthyroid subjects with high total concentrations of T4 in their sera have been studied (J.D.: T4, 170; T3, 1.90; rT3, 0.54 nmol/l. E.T.: T4, 185; T3, 1.63; rT3, 0.37 nmol/l). Concentrations of all three T4-binding proteins were within normal limits in both cases. However, on reverse-flow electrophoresis an abnormally large amount of thyroxine was found to travel with albumin. The three T4-binding proteins in the sera of both patients were separated from each other by a novel affinity chromatographic method using dye-Sepharose conjugates. Affinity constants for T4 binding to TBG and to prealbumin from both patients were normal. The albumin preparations were further purified and shown by physical and immunochemical techniques to be uncontaminated by other proteins. Scatchard plots of the binding of T4 to each of these pure albumins revealed two components, one having a normal affinity constant (J.D., 1.8 x 10(5) lmol-1 and E.T., 2.3 x 10(5) lmol-1), the other having a raised affinity constant (J.D., 5.4 x 10(6) lmol-1 and E.T., 5.8 x 10(6) lmol-1). Extrapolation of the plots showed that the high affinity components comprised 66% (J.D.) and 54% (E.T.) of the total purified albumin. The raised affinity and high concentrations ...Continue Reading

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