In vitro and in vivo iodination of human thyroglobulin in relation to hormone release

FEBS Letters

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

[1] Laboratoires de Chimie biologique et de Biochimie médicale Unité 38 INSERM, Faculté de Médecine, 27 Bd Jean Moulin, 13385 Marseille Cedex 5, France

关键词: Human thyroglobulin;    Hormonogenic site;    Thyroxine-containing peptide;    Proteolysis;    Iodination in vitro;   

DOI  :  10.1016/0014-5793(83)80252-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Reduced and S-alkylated thyroglobulin (Tgb) from different species were shown by SDS-PAGE to contain small peptides (from 45-9 kDA) rich in thyroxine. Several hypotheses were proposed to explain their origin. The polypeptide composition of iodine-poor (TgbA) and normally iodinated (Tgb B) human Tgb prepared by two different procedures (one minimizing and the other favoring post-mortem proteolysis) was compared in the native state and after in vitro iodination. Results show that one of the hormonogenic sites of human Tgb is part of a domain of the molecule most susceptible to proteolysis, especially when it is very iodinated.

【 授权许可】

Unknown