Cadmium-zinc interactions in the Ehrlich cell: metallothionein and other sites.
Cadmium-zinc interactions in the Ehrlich cell: metallothionein and other sites.
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艾利希细胞中的镉-锌相互作用：金属硫蛋白和其他位点。
DOI：
10.1007/978-3-0348-6784-9_59
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
Otvos,JD
中科院分区：
文献类型：
--
作者：
Petering,DH;Krezoski,S;Villalobos,J;Shaw3rd,CF;Otvos,JD
本文研究了培养的艾氏细胞中锌和镉的代谢。在EDTA或络合物限制胞外锌的条件下，碱性锌金属硫蛋白(MT)中的锌以0.35hr−1的速度从金属硫蛋白转移到其他位置。目前的研究表明，MT蛋白的生物降解速率常数为0.07-0.11hr−1，这意味着锌离开蛋白质的速度快于蛋白质的生物降解速度。在细胞暴露于17 ng Cd/mg细胞蛋白30分钟后，Cd最初取代了mt中的锌，并与高分子量物种结合。尽管细胞仍然活着，但细胞的增殖速度明显放缓。随着时间的推移，Cd转变为新合成的mt。这种蛋白质的表观速率常数是基础锌-Mt的四倍。该产品含有等量的镉和锌。然而，在镉被隔离在mt.
Zinc and Cadmium metabolism in cultured Ehrlich cells has been studied. Under conditions of restriction of extracellular zinc by EDTA or chelex, zinc in basal Zn-metallothionein (Mt) is transferred from metallothionein to other sites with a rate constant of 0.35 hr−1. Current studies indicate that the rate constant for biodegradation of Mt protein is 0.07–0.11 hr−1, implying that Zn leaves the protein faster than it is biodegraded. After a 30 minute exposure of cells to 17 ng atoms Cd/mg cell protein, Cd initially displaces Zn from Mt and binds to high molecular weight species. Cell proliferation is markedly slowed, although the cells remain viable. Over time Cd shifts into newly synthesized Mt. This protein is made with an apparent rate constant four times that for basal Zn-Mt. The product contains equal amounts of Cd and Zn. However, cell proliferation is not restored for many hours after Cd is sequestered in Mt.