THE STRUCTURE OF THYROID HORMONE PRECURSORS

甲状腺球蛋白解离为26,000道尔顿蛋白 琥珀酸化不会被糖蛋白用 三硝基苯磺酸(TNBS)。对正常人、人类的治疗 甲状腺球蛋白和TNBS单独引起大细胞的解离 糖蛋白转化为更小的多肽，其中一些具有分子 重量低至10,000。人19S甲状腺球蛋白的制备 地方性甲状腺肿不是通过三硝基苯基化解离的。因此， 甲状腺球蛋白的赖氨基残基可分为两部分： ~(19)S残存甲状腺球蛋白的赖氨基残基和~(10)S、~(10)O~(-) 道尔顿多肽很容易与TNBS反应，但不与TNBS反应 琥珀酸分析剂。然而，26,000的赖氨酰残留物 道尔顿多肽很容易与琥珀酸酐反应 在TNBS上表现不佳。

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.