Pedersen S M
Ann Rheum Dis. 1986 Sep;45(9):712-7. doi: 10.1136/ard.45.9.712.
The binding of aurothiomalate to human serum albumin was studied by equilibrium dialysis at 37 degrees C, pH 7.3-7.4, and ionic strength 0.15-0.16 mol/l. It was found that aurothiomalate was bound to albumin at one site with an apparent association constant K1 = 3.0 X 10(4) M-1 and at three or more sites with the sum of association constants of the order of 10(3) M-1. Valuable information of the aurothiomalate-albumin interaction was deduced from the observed changes of pH of the albumin solutions during dialysis. A conceivable binding mechanism consistent with the results might be that aurothiomalate binds as Au+ to the high affinity binding site by exchanging a H+ and that this site might be the sulphydryl group in cysteine34; and that aurothiomalate binds as monomeric anions to the lower affinity binding sites.
在37摄氏度、pH值7.3 - 7.4以及离子强度0.15 - 0.16 mol/l的条件下，通过平衡透析法研究了硫代苹果酸金钠与人血清白蛋白的结合情况。研究发现，硫代苹果酸金钠在一个位点与白蛋白结合，其表观缔合常数K1 = 3.0×10⁴ M⁻¹，并且在三个或更多位点结合，这些位点的缔合常数之和约为10³ M⁻¹。从透析过程中白蛋白溶液pH值的观测变化中，推断出了硫代苹果酸金钠 - 白蛋白相互作用的重要信息。与结果相符的一种可能的结合机制是，硫代苹果酸金钠以Au⁺形式通过交换一个H⁺与高亲和力结合位点结合，该位点可能是半胱氨酸34中的巯基；并且硫代苹果酸金钠以单体阴离子形式与低亲和力结合位点结合。
