| 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. |
