离子强度对硫代硫酸金钠与人血清白蛋白结合的影响。
Influence of ionic strength on the binding of sodium aurothiosulphate to human serum albumin.
作者信息
Pedersen S M
出版信息
Biochem Pharmacol. 1985 Dec 15;34(24):4319-23. doi: 10.1016/0006-2952(85)90291-6.
The effect of ionic strength on the binding of aurothiosulphate to human serum albumin has been studied at 37 degrees and neutral pH by equilibrium dialysis in unbuffered solutions. The effect of ionic strength is more pronounced on the lower association constants K2-K4 than on the high association constant K1. Furthermore a reduction in the number of lower affinity binding sites is observed at low ionic strength. The main ionic strength dependence on the association constants agrees with the Debye-Hückel theory. The extrapolated values of K1 and the sum of K2 to K4 at zero ionic strength are 7.6 X 10(5) M-1 and 1.1 X 10(5) M-1, respectively. It is shown that the observed changes in pH of the albumin solutions during dialysis contains valuable information of the aurothiosulphate-albumin interaction. A molecular binding mechanism is discussed.
在37摄氏度和中性pH条件下，通过在无缓冲溶液中进行平衡透析，研究了离子强度对金硫代硫酸盐与人血清白蛋白结合的影响。离子强度对较低的缔合常数K2 - K4的影响比对较高的缔合常数K1的影响更为显著。此外，在低离子强度下观察到较低亲和力结合位点的数量减少。离子强度对缔合常数的主要影响符合德拜 - 休克尔理论。在零离子强度下，K1的外推值以及K2到K4的总和分别为7.6×10⁵ M⁻¹和1.1×10⁵ M⁻¹。结果表明，透析过程中白蛋白溶液pH值的变化包含了金硫代硫酸盐 - 白蛋白相互作用的有价值信息。本文还讨论了一种分子结合机制。
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