Lanteigne D, Hnatowich D J
Int J Appl Radiat Isot. 1984 Jul;35(7):617-21. doi: 10.1016/0020-708x(84)90106-6.
We have determined that reduced 99mTc will often bind to proteins even in the presence of DTPA at reasonable concentrations. The extent of this competition varies with the protein but many possess this property. We have shown that, despite this competition, DTPA-coupled proteins can be labeled with 99mTc and that this labeling can be achieved at near-neutral pH using stannous ion for reduction. Both lysosyme and IgG antibody were labeled with 99mTc after coupling with DTPA and their biodistributions determined at 1-2 h in mice along with the 111In-labeled proteins as controls. The results of these animal studies show that the proteins are largely labeled at the DTPA sites and that they exhibit in vivo stabilities comparable to that of the 111In labeled proteins.
我们已经确定，即使在存在合理浓度二乙三胺五乙酸（DTPA）的情况下，还原态的99m锝（99mTc）通常也会与蛋白质结合。这种竞争的程度因蛋白质而异，但许多蛋白质都具有这种特性。我们已经表明，尽管存在这种竞争，DTPA偶联的蛋白质仍可以用99mTc进行标记，并且使用亚锡离子进行还原可以在接近中性的pH值下实现这种标记。溶菌酶和IgG抗体在与DTPA偶联后都用99mTc进行了标记，并在1至2小时内在小鼠体内测定了它们的生物分布，同时以111铟（111In）标记的蛋白质作为对照。这些动物研究的结果表明，蛋白质主要在DTPA位点被标记，并且它们在体内的稳定性与111In标记的蛋白质相当。
