Adylova A T, Atakhanova B A
Biokhimiia. 1986 Jan;51(1):112-7.
The interaction of thyroid hormones with rat liver nuclear matrix proteins was studied. It was shown that the nuclear matrix contains the sites which bind triiodothyronine with a high affinity (Ka = 1.07 X 10(9) M-1) and limited capacity (maximal binding capacity--28.5 fmol triiodothyronine/100 micrograms protein). Electrophoretic analysis of triiodothyronine-binding matrix proteins revealed that the molecular mass of the major triiodothyronine-binding fraction is 50 000-52 000 Da. Injections of triiodothyronine to thyroidectomized animals stimulated the phosphorylation of all protein fractions of the nuclear matrix.
研究了甲状腺激素与大鼠肝细胞核基质蛋白的相互作用。结果表明,核基质含有与三碘甲状腺原氨酸具有高亲和力(Ka = 1.07×10⁹ M⁻¹)且容量有限(最大结合容量——28.5 fmol三碘甲状腺原氨酸/100微克蛋白质)的结合位点。对三碘甲状腺原氨酸结合基质蛋白的电泳分析表明,主要的三碘甲状腺原氨酸结合组分的分子量为50000 - 52000 Da。给甲状腺切除的动物注射三碘甲状腺原氨酸可刺激核基质所有蛋白质组分的磷酸化。