par Vassart, Gilbert 
;Brocas, Huguette;Christophe, Daniel ;De Martynoff, Guy ;Leriche, Anne ;Mercken, Luc;Pohl, Viviane ;Van Heuverswyn, Brigitte
Référence Annales d'Endocrinologie, 43, page (404-414)
Publication Publié, 1982
;Brocas, Huguette;Christophe, Daniel ;De Martynoff, Guy ;Leriche, Anne ;Mercken, Luc;Pohl, Viviane ;Van Heuverswyn, Brigitte Référence Annales d'Endocrinologie, 43, page (404-414)
Publication Publié, 1982
Article révisé par les pairs
| Résumé : | Thyroglobulin is composed of two 300000 dalton polypeptide chains, translated from an 8000 base mRNA. Preparation of a full length cDNA and its cloning in E. coli have lead to the demonstration that the polypeptides of thyroglobulin protomers were identical. Used as molecular probes, the cloned cDNA allowed the isolation of a fragment of thyroglobulin gene. Electron microscopic studies have demonstrated that this gene contains more than 90% intronic material separating small size exons (less than 200 bp). Sequencing of bovine thyroglobulin structural gene is in progress. Preliminary results show evidence for the existence of repetitive segments. Availability of cloned DNA complementary to bovine and human thyroglobulin mRNA allows the study of genetic defects of thyroglobulin gene expression in the human and in various animal models. |
