Competitive binding of chromium, cobalt and nickel to serum proteins.
Competitive binding of chromium, cobalt and nickel to serum proteins.
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DOI：
10.1016/0142-9612(94)90049-3
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发表时间：
1994-03
期刊：
影响因子：
14
通讯作者：
Jim Yang;Jonathan Black
中科院分区：
文献类型：
--
作者：
Jim Yang;Jonathan Black
本文研究了铬、钴、镍三种氯化物盐与小鼠血清蛋白的竞争性结合。将单个金属盐溶液和组合与1：20稀释的鼠血清蛋白一起孵育24小时。然后通过透析除去游离金属。通过石墨炉原子吸收光谱法分析蛋白质结合的金属离子。本研究测定了钴和镍与血清蛋白的饱和结合。当以2摩尔金属对1摩尔白蛋白的浓度加入钴或镍时，小鼠血清几乎饱和。铬和钴具有相似的蛋白质结合亲和力，铬和钴与蛋白质的结合与添加的浓度比成比例。然而，镍显示出对铬和钴结合部分的显著竞争。本研究为今后腐蚀产物的生物学作用和性质研究提供了参考。
The competitive binding of chromium, cobalt and nickel chloride salts to murine serum proteins was studiedin vitro. Individual metal salt solutions and combinations were incubated with 1:20 dilution of murine serum proteins for 24 h. Then free metal was removed by dialysis. The protein bound metal ions were analysed by graphite furnace atomic absorption spectroscopy. This study determined the saturation binding of cobalt and nickel to serum proteins. Murine serum is mostly saturated when cobalt or nickel is added at the concentration of 2 mol of metal to 1 mol of albumin. Chromium and cobalt have similar protein binding affinity, chromium and cobalt bind to protein in proportion to the added concentration ratio. However, nickel shows significant competition for chromium and cobalt binding moieties. This study provides a reference for future research on the biological role and properties of corrosion products.