Characterization of a hormonogenic domain from human thyroglobulin

FEBS Letters

Rolland, Marcel¹  Lissitzky, Serge¹  Lejeune, Pierre-Jean¹  Marriq, Claudine¹  Venot, Nicole¹ 

[1] Laboratoire de Chimie Biologique, LA 178 CNRS et U 38 INSERM, Faculté de Médecine, 27 Bd Jean Moulin, 13385 Marseille Cédex 05, France

关键词: (Human);    Thyroglobulin;    Hormonogenic domain;    Iodination;    hTgb;    human thyroglobulin;    MIT;    3-iodotyrosine;    DIT;    3;    5-diiodotyrosine;    T4;    thyroxine;    T3;    3;    5;    3′-triiodothyronine;   

DOI  :  10.1016/0014-5793(86)81509-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A polypeptide domain of molecular mass near 22 kDa was purified from CNBr-digest of iodine poor human thyroglobulin (hTgb). This fragment represents the N-terminal part of the hTgb molecule and consequently contains the preferential hormonogenic tyrosine ‘acceptor’ of the protein. This fragment could correspond to the non-iodinated and unreduced form of the thyroxinyl-containing 26 kDa peptide previously purified from reduced and iodinated hTgb. This 22 kDa fragment is capable by itself, i.e. independently of the remaining hTgb molecule, of synthesizing thyroxine with a high efficiency after in vitro iodination. Its study should constitute a valuable way to identify at least one of the hormonogenic tyrosine ‘donor’ residues of hTgb.

【 授权许可】

Unknown