Irons R D, Smith J C
Arch Environ Contam Toxicol. 1977;6(2-3):193-202. doi: 10.1007/BF02097760.
Liver Cd-binding proteins (Cd-BP) were isolated from rats chronically treated with 109Cd-labeled CdCl2 for ten days. Fractions purified using Sephadex G-75 and DEAE-Sephadex were characterized and found to be similar to those isolated by other investigators. Cd-binding was not saturated in any of the preparations and significant amounts of Cu and Zn were also found bound to the proteins. The percentage of saturation of Cd-BP1, and Cd-BP2 was independently determined by atomic absorption spectrometry and spectroscopy at 254 nm. These results indicate that the fraction of binding sites unoccupied by Cd on Cd-BP approaches 20% in vivo.
从用¹⁰⁹Cd标记的氯化镉慢性处理十天的大鼠中分离出肝脏镉结合蛋白（Cd-BP）。使用葡聚糖凝胶G-75和二乙氨基乙基葡聚糖纯化的组分经过表征，发现与其他研究者分离的组分相似。在任何制剂中镉结合都未饱和，并且还发现大量的铜和锌也与这些蛋白质结合。通过原子吸收光谱法和254nm处的光谱法独立测定了Cd-BP1和Cd-BP2的饱和百分比。这些结果表明，在体内Cd-BP上未被镉占据的结合位点比例接近20％。
