Yang J, Black J
Department of Bioengineering, Clemson University, SC 29634-0905.
Biomaterials. 1994 Mar;15(4):262-8. doi: 10.1016/0142-9612(94)90049-3.
The competitive binding of chromium, cobalt and nickel chloride salts to murine serum proteins was studied in 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.
体外研究了氯化铬、氯化钴和氯化镍盐与小鼠血清蛋白的竞争性结合。将单独的金属盐溶液及其组合与稀释20倍的小鼠血清蛋白一起孵育24小时。然后通过透析去除游离金属。通过石墨炉原子吸收光谱法分析与蛋白质结合的金属离子。本研究确定了钴和镍与血清蛋白的饱和结合情况。当以2摩尔金属比1摩尔白蛋白的浓度添加钴或镍时，小鼠血清大多处于饱和状态。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比例与添加浓度成正比。然而，镍对铬和钴的结合部分表现出显著的竞争。本研究为未来关于腐蚀产物的生物学作用和性质的研究提供了参考。
