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Clinical Chemistry 20: 1150-1154, 1974;
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Clinical Chemistry, Vol 20, 1150-1154, Copyright © 1974 by the American Association for Clinical Chemistry

Radioimmunoassay for Serum Triiodothyronine: Evaluation of Simple Techniques to Control Interference from Binding Proteins

Victor S. Fang 1 and Samuel Refetoff 1

1 Endocrinology Section, Department of Medicine, The University of Chicago, Chicago, Ill. 60637.

Simple techniques for controlling interference from binding proteins in serum, such as thyroxine-binding globulin, in radioimmunoassay for triiodothyronine (T3) have been evaluated for their efficacy, and their effect on assay sensitivity and on recovery of added T3. Ethanol precipitation of serum proteins decreased the assay sensitivity, nonspecific binding was increased, and recoveries of added T3 were inconsistent. Heat-inactivation of thyroxine-binding globulin or use of 8-anilino-1naphthalene sulfonic acid (ANS) to displace T3 from thyroxine-binding globulin produced comparable recovery rates. The heat-inactivation method slightly decreased the sensitivity of the assay and prolonged the procedure, whereas use of ANS is simple, and the assay sensitivity is maintained. When sera contain a high concentration of thyroxine-binding globulin, a fixed concentration of ANS (175 µg/100 µl of serum) might be too low to displace T3 from all its binding sites, but a concentration of ANS greater than 200 µg/100 µl of serum interferes with T3 quantitation by competitively binding to the antibodies. The cross-reactivity of thyroxine to T3-antibodies varies with the antiserum. Thyroxine-binding globulin appears to be the only protein in serum that competes with the antibody for T3 binding.


Key Words: ethanol-precipitation or heat-inactivation of thyroxine-binding globulin and use of 8-anilino-1-naphthalene sulfonic acid compared

Submitted on April 3, 1974
Accepted on June 11, 1974




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