Lennon A M, Chantoux F, Osty J, Francon J
Biochem Biophys Res Commun. 1983 Nov 15;116(3):901-8. doi: 10.1016/s0006-291x(83)80227-7.
A thyroid hormone binding protein(s) has been characterized in the cytosol of fetal rat brain cells in primary cultures. This protein is closely related to the one described in brain supernatants with respect to its electrophoretic mobility, binding kinetic parameters and estimated molecular weight (65 000 daltons). However, in contrast to the brain cytosolic binding protein, two classes of affinity sites for triiodothyronine (T3) and thyroxine (T4) have been demonstrated: a high affinity site (KA = 1.2-3.7(3) X 10(9) M-1 for T3 and KA = 3.7-5 X 10(8) M-1 for T4) and a low affinity site (KA = 0.8-1.4 X 10(8) M-1 for T3 and 1.6-2.9 X 10(7) M-1 for T4). The results are discussed with respect to their cellular significance.
在原代培养的胎鼠脑细胞胞质溶胶中已鉴定出一种甲状腺激素结合蛋白。就其电泳迁移率、结合动力学参数和估计分子量(65000道尔顿)而言,这种蛋白与脑上清液中描述的蛋白密切相关。然而,与脑胞质溶胶结合蛋白不同,已证明存在两类三碘甲状腺原氨酸(T3)和甲状腺素(T4)的亲和位点:一个高亲和位点(T3的KA = 1.2 - 3.7(3)×10(9) M-1,T4的KA = 3.7 - 5×10(8) M-1)和一个低亲和位点(T3的KA = 0.8 - 1.4×10(8) M-1,T4的KA = 1.6 - 2.9×10(7) M-1)。对这些结果的细胞意义进行了讨论。