Woods M, Mason J
Biochemistry Department, Trinity College, Dublin, Ireland.
J Inorg Biochem. 1987 Aug;30(4):261-72. doi: 10.1016/0162-0134(87)80070-3.
Spectral studies showed that copper and trithiomolybdate participated in a three-way interaction with bovine and canine serum albumin. The interaction with the proteins was affected by increased pH and ionic strength. Kinetic studies of binding equilibria indicated that [35S] trithiomolybdate bound to both albumins at a single site. The affinity of the site, but not the capacity of the protein, was increased by copper. It was concluded that the site was distinct from the N-terminal copper (and nickel) binding site, which is present on BSA but absent from CSA. Whether or not the N-terminal site has a role in copper transport is discussed. Reversible thiomolybdate-copper-protein interactions of this type may play a fundamental role in the pathogenesis of Mo-induced syndromes, since as the normal binding patterns are perturbed the interprotein equilibria are altered and the copper distribution patterns are modified.
光谱研究表明，铜和三硫代钼酸盐与牛血清白蛋白和犬血清白蛋白发生三方相互作用。与蛋白质的相互作用受pH值升高和离子强度的影响。结合平衡的动力学研究表明，[35S]三硫代钼酸盐在单个位点与两种白蛋白结合。铜增加了该位点的亲和力，但不影响蛋白质的结合容量。得出的结论是，该位点与N端铜（和镍）结合位点不同，后者存在于牛血清白蛋白上，但不存在于犬血清白蛋白上。文中讨论了N端位点是否在铜转运中起作用。这种可逆的硫代钼酸盐-铜-蛋白质相互作用可能在钼诱导综合征的发病机制中起重要作用，因为随着正常结合模式受到干扰，蛋白质间平衡发生改变，铜分布模式也会被改变。
