Vassart G, Refetoff S, Brocas H, Dinsart C, Dumont J E
Proc Natl Acad Sci U S A. 1975 Oct;72(10):3839-43. doi: 10.1073/pnas.72.10.3839.
Thyroglobulin is a 19S protein of approximately 660,000 daltons and unknown quaternary structure. We have previously shown that a 33S mRNA purified from mammalian thyroids promoted synthesis in the Xenopus oocyte of a peptide immunologically related to thyroglobulin. Chemical identity to the native protein is now presented by means of a tryptic peptide analysis. Moreover, the 33S mRNA is shown to contain all the information required for the synthesis of a complete 19S thyroglobulin molecule. Gel filtration in Sepharose under denaturing conditions indicates that the reduced polypeptide encoded by the 33S mRNA is larger than 210,000 daltons. A model of a dimeric thyroglobulin with about 300,000 dalton subunits is presented.
甲状腺球蛋白是一种分子量约为660,000道尔顿的19S蛋白质,其四级结构未知。我们之前已经表明,从哺乳动物甲状腺中纯化得到的33S mRNA能促进非洲爪蟾卵母细胞合成一种与甲状腺球蛋白具有免疫相关性的肽。现在通过胰蛋白酶肽段分析确定了其与天然蛋白质的化学一致性。此外,33S mRNA被证明包含合成完整的19S甲状腺球蛋白分子所需的所有信息。在变性条件下于琼脂糖凝胶过滤表明,由33S mRNA编码的还原多肽分子量大于210,000道尔顿。本文提出了一种由约300,000道尔顿亚基组成的二聚体甲状腺球蛋白模型。