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Over half a century ago it was demonstrated that circulating thyroid hormones are non-covalently bound to plasma proteins (1). Unbound hormone now is accepted generally as the major direct determinant of biological activity (2) and its estimation is diagnostically superior to the measurement of total hormone, especially where the concentration of binding proteins is altered owing to hereditary or acquired variations. However, there is a notable lack of consensus as to how the free thyroid hormone concentration should be measured. Despite ingenious efforts to make free T4 measurements simple and reliable, detailed examination of currently available techniques suggests that there is no perfect method, especially when the effects of dilution or potential inhibitors of plasma protein binding are considered (3).
It is fundamental to the free hormone concept that the protein-bound moiety serves as a reservoir of "stored" hormone that dissociates progressively in vitro as the sample is diluted,
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R. Sapin, J.-L. Schlienger, F. Gasser, E. Noel, B. Lioure, F. Grunenberger, B. Goichot, and D. Grucker Intermethod Discordant Free Thyroxine Measurements in Bone Marrow-transplanted Patients Clin. Chem., March 1, 2000; 46(3): 418 - 422. [Full Text] [PDF] |
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