Lejeune P J, Marriq C, Rolland M
Laboratoires de Chimie biologique et de Biochimie médicale associés au C.N.R.S., U.A. n. 178 et U. n. 38 de l'I.N.S.E.R.M., Faculté de Médecine, Marseille.
C R Acad Sci III. 1988;307(3):123-7.
Normally iodinated thyroglobulin (Tg) contains low molecular weight hormone-rich peptides associated to the bulk of the molecule by disulfide bridges. It is shown, with the assistance of in vitro iodination experiments using different iodine concentrations and various incubation times, that the proteolytic cleavage giving rise to the 26 K hormonopeptide in human Tg is part of a coupling reaction rather than iodination. This cleavage may be a preliminary event related to a facilitation in the release of thyroid hormones.
正常情况下，碘化甲状腺球蛋白（Tg）含有低分子量的富含激素的肽段，这些肽段通过二硫键与分子主体相连。通过使用不同碘浓度和不同孵育时间的体外碘化实验表明，人Tg中产生26K激素肽的蛋白水解切割是偶联反应的一部分，而非碘化反应。这种切割可能是与促进甲状腺激素释放相关的一个初步事件。
