[C-terminal extremity of ovine thyroglobulin shows strong interspecies homologies].
We report on the 466 nucleotides long, extreme 3' end of the ovine thyroglobulin (Tg) mRNA. The nucleotide sequence and the deduced carboxyl terminal region of the protein have been compared with those reported in other species. Comparison with hog peptides known to contain all the triiodothyronine (T3) of the mature Tg suggests that the antepenultimate amino acid, a tyrosine residue could be involved in hormone formation. This also agree with the data reported for bovine and murine Tg.
D000818:Animals; D001483:Base Sequence; D002417:Cattle; D004247:DNA / Q000648:ultrastructure; D008969:Molecular Sequence Data; D010443:Peptide Chain Termination, Translational; D012333:RNA, Messenger / Q000648:ultrastructure*; D051381:Rats; D012756:Sheep; D013045:Species Specificity; D013552:Swine; D013954:Thyroglobulin / Q000032:analysis* / Q000096:biosynthesis; D014284:Triiodothyronine / Q000096:biosynthesis
D012333:RNA, Messenger; D014284:Triiodothyronine; D004247:DNA; D013954:Thyroglobulin
L'extrémité C-terminale de la thyroglobuline ovine présente de fortes homologies interspécifiques.