Samuels H H, Tsai J S, Casanova J
Science. 1974 Jun 14;184(4142):1188-91. doi: 10.1126/science.184.4142.1188.
Saturable binding activities for triiodothyronine were demonstrated in vitro with isolated nuclei and soluble nuclear extracts of rat liver, kidney, and cultured GH(1) cells. The binding activity can be extracted from nuclei in soluble form with no significant change in hormone affinity and has properties of a nonhistone protein.
在体外,用大鼠肝脏、肾脏和培养的GH(1)细胞的分离细胞核及可溶性核提取物证实了三碘甲状腺原氨酸的饱和结合活性。该结合活性可以以可溶形式从细胞核中提取出来,激素亲和力无显著变化,并且具有非组蛋白的特性。