Mercken L, Simons M J, Vassart G
FEBS Lett. 1982 Nov 29;149(2):285-7. doi: 10.1016/0014-5793(82)81118-6.
The sequence of 370 bases at the 5'-end of bovine thyroglobulin mRNA has been determined. A 41 base untranslated segment was found preceeding the ATG initiator codon. It is followed by an open reading frame providing the first data on thyroglobulin primary structure. Analysis of the amino acid sequence demonstrated the presence of an 18 residue hydrophobic segment representing a putative signal peptide. Comparison of the amino terminal sequence of thyroglobulin with that of peptides known to contain thyroid hormones [7,8] demonstrated that the first tyrosine in native thyroglobulin is mainly found as thyroxine in the mature iodinated protein [8]. Our results clearly identify the amino-terminal region of thyroglobulin as an important hormonogenic domain of the protein.
已确定牛甲状腺球蛋白mRNA 5'端370个碱基的序列。在ATG起始密码子之前发现了一个41个碱基的非翻译片段。随后是一个开放阅读框，提供了有关甲状腺球蛋白一级结构的首批数据。对氨基酸序列的分析表明存在一个18个残基的疏水片段，代表一个假定的信号肽。将甲状腺球蛋白的氨基末端序列与已知含有甲状腺激素的肽的序列进行比较[7,8]，结果表明天然甲状腺球蛋白中的第一个酪氨酸在成熟的碘化蛋白中主要以甲状腺素的形式存在[8]。我们的结果清楚地确定甲状腺球蛋白的氨基末端区域是该蛋白质的一个重要激素生成结构域。
