Abstract
Interactions between two human iodothyronine-binding autoantisera and three preparations of human thyroglobulin (Tg) were not proportional to the latter's thyroxyl residue content. Probably only one of the several thyroxyl-containing sites in Tg reacted with the immunoglobulins from both antisera. In the case of one of the antisera, which was thyroxine (T4)-specific, the thyroxyl residue was the immunodominant feature of the antigenic site. The other antiserum, which had a specificity for 3,5,3'-tri-iodothyronine (T3), recognized different determinants around the same thyroxyl residue, but this residue was not itself an important element of the binding site. Thus, despite the specificity for T3 free in solution, the presence of T4 in the complete antigenic site was tolerated, since other structures supplied the bulk of the binding energy. 'Specificity' of this antiserum for T3 in solution is therefore coincidental and need not be ascribed to the presence of T3 in the original immunogen. Some results obtained in these studies may be interpreted as supporting the possibility that a modified Tg was the immunogen for the generation of these naturally occurring human antisera.
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Selected References
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- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
- Deme D., Gavaret J. M., Pommier J., Nunez J. Maximal number of hormonogenic iodotyrosine residues in thyroglobulin iodinated by thyroid peroxidase. Eur J Biochem. 1976 Nov 1;70(1):7–13. doi: 10.1111/j.1432-1033.1976.tb10949.x. [DOI] [PubMed] [Google Scholar]
- Gavaret J. M., Dème D., Nunez J., Salvatore G. Sequential reactivity of tyrosyl residues of thyroglobulin upon iodination catalyzed by thyroid peroxidase. J Biol Chem. 1977 May 25;252(10):3281–3285. [PubMed] [Google Scholar]
- Lamas L., Taurog A., Salvatore G., Edelhoch H. Preferential syntheisi of thyroxine from early iodinated tyrosyl residues in thyroglobulin. J Biol Chem. 1974 May 10;249(9):2732–2737. [PubMed] [Google Scholar]
- Marriq C., Arnaud C., Rolland M., Lissitzky S. An approach to the structure of thyroglobulin. Hormone-forming sequences in porcine thyroglobulin. Eur J Biochem. 1980 Oct;111(1):33–47. doi: 10.1111/j.1432-1033.1980.tb06072.x. [DOI] [PubMed] [Google Scholar]
- Maurizis J. C., Marriq C., Rolland M., Lissitzky S. Thyroid hormone synthesis and reactivity of hormone-forming tyrosine residues of thyroglobulin. FEBS Lett. 1981 Sep 14;132(1):29–32. doi: 10.1016/0014-5793(81)80420-6. [DOI] [PubMed] [Google Scholar]
- ORNSTEIN L. DISC ELECTROPHORESIS. I. BACKGROUND AND THEORY. Ann N Y Acad Sci. 1964 Dec 28;121:321–349. doi: 10.1111/j.1749-6632.1964.tb14207.x. [DOI] [PubMed] [Google Scholar]
- Ochi Y., Shiomi K., Hachiya T., Yoshimura M., Miyazaki T. Immunological analysis of abnormal binding of thyroid hormone in the gamma globulin. J Clin Endocrinol Metab. 1972 Nov;35(5):743–752. doi: 10.1210/jcem-35-5-743. [DOI] [PubMed] [Google Scholar]
- Pearce C. J., Byfield P. G., Edmonds C. J., Lalloz M. R., Himsworth R. L. Autoantibodies to thyroglobulin cross reacting with iodothyronines. Clin Endocrinol (Oxf) 1981 Jul;15(1):1–10. doi: 10.1111/j.1365-2265.1981.tb02741.x. [DOI] [PubMed] [Google Scholar]
- Pitt-Rivers R. The subunit structure of thyroglobulin. Biochem J. 1976 Sep 1;157(3):767–768. doi: 10.1042/bj1570767. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rolland M., Montfort M. F., Lissitzky S. Efficiency of thyroglobulin as a thyroid hormone-forming protein. Biochim Biophys Acta. 1973 Apr 20;303(2):338–347. doi: 10.1016/0005-2795(73)90365-6. [DOI] [PubMed] [Google Scholar]
- Vignal A., Nataf B. M., Tubiana M. Iodoamino acid composition of poorly iodinated human thyroglobulin fractionated by isopycnic centrifugation. Acta Endocrinol (Copenh) 1978 Feb;87(2):320–329. doi: 10.1530/acta.0.0870320. [DOI] [PubMed] [Google Scholar]