Translation of thyroglobulin 33S messenger RNA as a means of determining thyroglobulin quaternary structure.
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.
D000818:Animals; D001001:Anura; D005260:Female; D046911:Macromolecular Substances; D008970:Molecular Weight; D009865:Oocytes / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D011233:Precipitin Tests; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012333:RNA, Messenger / Q000378:metabolism*; D013954:Thyroglobulin / Q000096:biosynthesis / Q000276:immunology; D014357:Trypsin; D014981:Xenopus
D046911:Macromolecular Substances; D010446:Peptide Fragments; D012333:RNA, Messenger; D013954:Thyroglobulin; D014357:Trypsin