Binding of cadmium ions by rat liver and kidney.
Binding of cadmium ions by rat liver and kidney.
复制标题
大鼠肝脏和肾脏对镉离子的结合。
DOI：
10.1016/0006-2952(72)90023-8
复制
发表时间：
1972
影响因子：
5.8
通讯作者：
M. Webb
中科院分区：
文献类型：
--
作者：
M. Webb
成年大鼠皮下注射CdCl_2（2.2 μ mol/100 g体重）后，其肝脏和肾脏中积累的大部分结合态Cd ~（2+）从这些组织的可溶性组分中以单一的热稳定组分形式回收。虽然这一部分在任何器官也结合Zn 2+，Cd 2+不取代Zn 2+从任何正常的，可溶性Zn 2 +-metalloprotein.The蛋白质的肝脏和肾脏积累Cd 2+似乎并不相同，但有共同的属性和之后，但不是之前去除结合阳离子富含-SH基团。至少在雄性大鼠中，这些Cd 2+结合蛋白不是这些组织的正常成分，而是响应于外来阳离子的摄取而合成的。在肝脏中，这种合成似乎在翻译水平上受到控制，因为它被放线菌酮抑制，但不被放线菌素D抑制。同样在肝脏中，相同蛋白质的合成由过量的Zn 2+诱导，而不是由Co 2+、Ni 2+和Pb 2+诱导，并且“结合蛋白”可能在Zn 2+代谢的控制中正常起作用。它们的诱导由Cd 2+和Hg 2+，因此可能是这些阳离子和Zn 2+的化学性质的相似性的结果。
Most of the bound Cd2+, which accumulates in the livers and kidneys of adult rats after the subcutaneous injection of CdCl2(2·2 μmoles/100 g body wt) is recovered as a single, heat-stable fraction from the soluble components of these tissues. Although this fraction in either organ also binds Zn2+, Cd2+does not displace Zn2+from any of the normal, soluble Zn2+-metalloproteins.The proteins of liver and kidney that accumulate Cd2+do not appear to be identical, but have properties in common and after, but not before removal of the bound cations are rich in —SH groups. At least in the male rat, these Cd2+-binding proteins are not normal components of these tissues but are synthesized in response to the uptake of the foreign cation. In the liver, this synthesis seems to be controlled at the translational level, since it is inhibited by cycloheximide, but not by actinomycin D. Also in the liver, the synthesis of the same protein is induced by excess Zn2+, but not by Co2+, Ni2+and Pb2+and it is possible that the “binding proteins” normally function in the control of Zn2+-metabolism. Their induction by Cd2+and also by Hg2+, thus may be a consequence of the similarities in the chemical properties of these cations and of Zn2+.