Weiner R E, Schreiber G J, Hoffer P B
J Nucl Med. 1983 Jul;24(7):608-14.
Equilibrium dialysis was used to examine the binding of Ga-67 to horse spleen ferritin (HFE), and the ability of this protein to remove Ga-67 originally bound to human transferrin (TF). Seventy hours were required for the HFE to bind 70% of the activity. When HFE was placed in competition with preformed TF-Ga-67 complex, little nuclide was translocated to HFE. Upon the addition of compounds of low molecular weight that occur intracellularly, this transfer was dramatically enhanced. In the presence of 1 mM adenosine triphosphate (ATP), the most effective mediator examined, the final distribution was 17% bound to TF and 62% to HFE, with 16% not protein-bound. In the absence of any mediator, the same distribution was 84, 6, and 3%. Control experiments with ATP showed that little radionuclide was transferred from TF to albumin. These results add support to the previous suggestions of the potential role of ferritin in Ga-67 localization.
采用平衡透析法研究了镓-67与马脾铁蛋白（HFE）的结合情况，以及该蛋白去除原本与人类转铁蛋白（TF）结合的镓-67的能力。HFE需要70小时才能结合70%的活性。当HFE与预先形成的TF-镓-67复合物竞争时，很少有核素转移到HFE上。加入细胞内存在的低分子量化合物后，这种转移显著增强。在1 mM三磷酸腺苷（ATP）（所检测的最有效的介质）存在的情况下，最终分布为17%与TF结合，62%与HFE结合，16%未与蛋白质结合。在没有任何介质的情况下，相同的分布分别为84%、6%和3%。用ATP进行的对照实验表明，很少有放射性核素从TF转移到白蛋白上。这些结果为先前关于铁蛋白在镓-67定位中潜在作用的建议提供了支持。
