Thyroxine-rich iodopeptides as fragment of reduced guinea pig thyroglobulin.
Full reduction of guinea pig thyroglobulin with mercaptoethanol followed by polyacrylamide gel electrophoresis reveals the presence besides the well known three polypeptide chains, of small amounts of iodopeptides with a molecular weight of 3 000 to 46 000 daltons. One of these peptides with a molecular weight of roughly 10 000 daltons has a much higher efficiency to couple iodotyrosines into thyroxine than any other fragment of thyroglobulin. Despite its small quantity this peptide contributes more than one third to the total thyroxine synthesis from a given iodide shot at any time up to five days after its injection. Iodopeptides akin to that found in guinea pigs were recently described by several authors in different species. They probably represent the preferential domains for hormone synthesis within the intact thyroglobulin molecule.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D007467:Iodoproteins / Q000032:analysis* / Q000378:metabolism; D008623:Mercaptoethanol; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis*; D013954:Thyroglobulin / Q000032:analysis*; D013974:Thyroxine / Q000096:biosynthesis*
D007467:Iodoproteins; D010446:Peptide Fragments; D008623:Mercaptoethanol; D013954:Thyroglobulin; D013974:Thyroxine