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Clinical Chemistry 34: 1745-1748, 1988;
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Clinical Chemistry, Vol 34, 1745-1748, Copyright © 1988 by American Association for Clinical Chemistry

Detection of protein binding abnormalities in euthyroid hyperthyroxinemia

PM George, JM Sheat and BN Palmer
Department of Clinical Biochemistry, Christchurch Hospital, New Zealand.

This is a procedure for rapidly identifying the three common abnormalities in binding of thyroxin by protein. After incubation with [125I]thyroxin, serum proteins are separated by electrophoresis on agarose gel and binding of thyroxin to the various protein fractions is determined after autoradiography. Quantitatively abnormal binding to albumin or prealbumin and thyroxin autoantibodies is easily demonstrated by this technique. Normally, less than 6% is bound to albumin, and no binding by prealbumin is detected. In dysalbuminemic hyperthyroxinemia, about 30% of the serum thyroxin is bound to albumin; in prealbumin-associated hyperthyroxinemia, 7% is bound to prealbumin. With this procedure these protein-binding abnormalities can be simply identified, and it may be useful when results of a thyroxin assay are not consistent with results of a sensitive thyrotropin assay or the patient's clinical examination.


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S. J. Cameron, J. C. Hagedorn, L. J. Sokoll, P. Caturegli, and P. W. Ladenson
Dysprealbuminemic Hyperthyroxinemia in a Patient with Hyperthyroid Graves Disease
Clin. Chem., June 1, 2005; 51(6): 1065 - 1069.
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