Precursor‐product relationship between the 26‐kDa and 18‐kDa fragments formed by iodination of human thyroglobulin

FEBS Letters

Rolland, Marcel¹  Lissitzky, Serge²  Lejeune, Pierre-Jean¹  Marriq, Claudine²  Malthiery, Yves² 

[1] Laboratoire de Chimie Biologique, Faculté de Médecine, 27 Bd. Jean Moulin, 13385 Marseille Cédex 05, France;Laboratoire de Biochimie Médicale associé au CNRS (LA 178), Unité 38 de l'INSERM Marseille Cédex 05, France

关键词: Human thyroglobulin;    Thyroxine-containing peptide;    Peptide structure;    HPLC;    In vitro iodination;    hTgb;    human thyroglobulin;    MIT;    3-iodotyrosine;    DIT;    3;    5-diiodotyrosine;    T4;    thyroxine;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/0014-5793(84)80587-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

At moderate iodination levels (20 iodine at atoms/molecule), human thyroglobulin (hTgb) produces after reduction a thyroxinyl-peptide of 26 kDa which represents the N-terminal part of the protein. At higher iodination levels, the 26-kDa peptide is accompanied by another T₄-containing peptide of 18 kDa. A precursor-product relationship between the 26- and 18-kDa fragments was demonstrated by the study of the tryptic fragments of both hormonopeptides. In addition, comparison with the protein sequence deduced from the nucleotide sequence of the 5'-end of hTgb mRNA demonstrated that the N-terminal region of Htgb from which are issued the 26-kDa peptide and its 18-kDa derivative is especially sensitive to proteolysis. This character is possibly related with a facilitated release of thyroid hormones in vivo.

【 授权许可】

Unknown