Iodoamino Acid Composition of Poorly Iodinated Human Thyroglobulin Fractionated by Isopycnic Centrifugation

Vignal, A; Nataf, B; Tubiana, M

doi:10.1530/acta.0.0870320

Cited by 9 publications

(1 citation statement)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Direct analytical methods applied to Tg preparations from several species have shown that, in general, the first tyrosine residues to be iodinated are also the first to couple into iodothyronines (Lamas et al, 1974;Deme et al, 1976;Gavaret et al, 1977;Vignal et al, 1978) and that the different thyroxyls in Tg are synthesized in an order that is controlled by the tertiary structure of the protein (Rolland et al, 1972;Lamas et al, 1974;Deme et al, 1976;Gavaret et al, 1977;Maurizis et al, 1981). It is implicit in these observations that the iodothyronine-synthesizing sites in Tg differ in some way.…”

Section: Discussionmentioning

confidence: 99%

Restricted antigenicity of thyroxyls in human thyroglobulin

Byfield¹,

Bond²,

Copping³

et al. 1982

Biochemical Journal

View full text Add to dashboard Cite

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.

show abstract