Nov 10, 1976

Binding of thyroid hormones and their analogues to thyroxine-binding globulin in human serum

The Journal of Biological Chemistry
S M SnyderE C Jorgensen

Abstract

The present study was undertaken to study the binding of several thyroid hormones and structurally related compounds to human serum thyroxine-binding alpha-globulin (TBG). The source of TBG was normal human serum diluted 1:100 in 0.035 M barbital buffer, pH 7.4. In the binding assays, 125I-thyroxine, unlabeled thyroxine, and diluted serum were incubated for 20 h at 37 degrees in Plexiglas equilibrium dialysis units. Two orders of binding sites were discerned: a high affinity, low capacity binding site with an affinity constant of approximately 2.5 X 10(9) M-1, and a low affinity, very high capacity binding site with an affinity constant of less than 10(6) M-1. Studies with purified TBG, serum deficient in TBG, and purified human serum albumin indicated that the high affinity site represented binding to TBG and the low affinity site represented binging to albumin. The ability of several groups of thyroid hormone analogues to bind to TBG was then investigated. As a result of these studies, the following structural features of thyroid hormones were found to be important for optimal binding activity: (a) the L-alanine side chain conformation, (b) the presence of a 4'-hydroxyl group, (c) the presence of two substituents in the inner...Continue Reading

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Mentioned in this Paper

Plexiglas
Novothyral
Thyroxine-Binding Globulin
Structure-Activity Relationship
Iodine, Homeopathic preparation
ALB
Albumin Human, USP
Thyroxine Measurement
Ethers
Human Serum Albumin [EPC]

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