Savu L, Vranckx R, Maya M, Nunez E A
U. 224, INSERM-Faculté de Médecine Xavier Bichat, Paris.
Biochem Biophys Res Commun. 1987 Nov 13;148(3):1165-73. doi: 10.1016/s0006-291x(87)80255-3.
We report evidence based on equilibrium binding, electrophoretic, autoradiographic studies, that the rat possesses a major high affinity thyroid hormone binding protein, with an electrophoretic mobility and binding properties similar to those of the human thyroxine binding globulin (TBG). We show that in the sera of postnatal developing animals, the thyroxine and the triiodothyronine binding activities increase up to 10 times over adult or foetal levels, due to a high transient post-natal surge of the rat TBG. In the adult serum, the TBG persists in decreased amounts: it then yields the predominant role as thyroxine carrier to the thyroid binding prealbumin, but retains the major role as binder of triiodothyronine i.e. of the biologically active thyroid hormone.
我们报告了基于平衡结合、电泳和放射自显影研究的证据，即大鼠拥有一种主要的高亲和力甲状腺激素结合蛋白，其电泳迁移率和结合特性与人类甲状腺素结合球蛋白（TBG）相似。我们发现，在出生后发育动物的血清中，甲状腺素和三碘甲状腺原氨酸结合活性比成年或胎儿水平增加了10倍，这是由于大鼠TBG在出生后出现了高瞬时激增。在成年血清中，TBG的含量持续减少：它作为甲状腺素载体的主要作用让位给甲状腺结合前白蛋白，但保留了作为三碘甲状腺原氨酸（即生物活性甲状腺激素）结合剂的主要作用。
