Abstract
Summary and conclusions
1. Serum from 6 patients who had received radioiodide or I131-labeled thyroxine was studied by zone electrophoresis in filter paper, at pH 8.6. Most of the I131 had a mobility intermediate between the alpha1- and alph2-glabulins, and a small proportion had the mobility of albumin. No differences were detected between thyroxine added to serum (in vivo) and the thyroid hormone secreted by a normal thyroid gland, by a Graves' disease thyroid gland, and by a functioning thyroid carcinoma. 2. Two patients had received very large doses of radio-iodide and their serum contained large amounts of butanol-insoluble I131, whereas in the other patients the serum I131 was largely butanol soluble, and behaved like thyroxine on paper chromatography. These two forms of serum I131 had similar mobility on zone electrophoresis, but could be differentiated by fractional precipitation of the serum proteins with phosphate buffer. The radioiodine, therefore, was probably attached, in each instance, to a different protein, and the identity in their mobilities was fortuitous. 3. Zone electrophoresis of purified hog thyroglobulin, and of I131-labeled rat thyroglobulin in a crude thyroid extract, revealed that these substances also had a mobility in the range of the alpha globulins of human serum. This finding is compatible with the previous suggestion that the butanol-insoluble I131 (“non-thyroxine I131”) may be thyroglobulin, released into the circulation from damaged thyroid tissue.
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