THE STRUCTURE OF THYROID HORMONE PRECURSORS

甲状腺球蛋白解离为26，000-道尔顿蛋白 琥珀酰化不被用以下物质预处理糖蛋白所阻断： 三硝基苯磺酸（TNBS）。 正常人的治疗 甲状腺球蛋白与TNBS单独引起大的 糖蛋白分解成较小的肽，其中一些具有分子 重量低至10，000。 从人制备的19 S甲状腺球蛋白 地方性甲状腺肿与三硝基苯化无关。 因此，在本发明中， 甲状腺球蛋白的赖氨酰残基可分为两部分： 19 S残留甲状腺球蛋白的赖氨酰残基和10，000- 道尔顿肽容易与TNBS反应，但不与TNBS反应。 琥珀酸分析物。 然而，26000个赖氨酸残基 道尔顿肽容易与琥珀酸酐反应， 与TNBS差。

Dissociation of thyroglobulin to a 26,000-dalton protein by succinylation is not blocked by pretreating the glycoprotein with trinitrobenzenesulfonic acid (TNBS). Treatment of normal, human thyroglobulin with TNBS alone causes dissociation of the large glycoprotein into smaller peptides some of which have molecular weights as low as 10,000. 19S thyroglobulin prepared from a human endemic goiter is not dissociated by trinitrophenylation. Thus, the lysyl residues of thyroglobulin can be divided into two parts: the lysyl residues of 19S residual thyroglobulin and of the lO,OOO- dalton peptide react readily with TNBS but do not react with succinic analyaride. However, the lysyl residues of the 26,000 dalton peptide react readily with succinic anhydride and react poorly with TNBS.