Open AccessTranslation of thyroglobulin 33S messenger RNA as a means of determining thyroglobulin quaternary structure.
Author(s) -
Gilbert Vassart,
Samuel Refetoff,
Huguette Brocas,
Christiane Dinsart,
Jacques Emile Dumont
Publication year - 1975
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.10.3839
Subject(s) - thyroglobulin , messenger rna , xenopus , ribosome , chemistry , translation (biology) , biochemistry , rna , molecular mass , protein quaternary structure , sepharose , microbiology and biotechnology , peptide , biology , thyroid , protein subunit , enzyme , endocrinology , gene
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.