Luĭk A I, Luk'ianchuk V D
Vopr Med Khim. 1982 Sep-Oct;28(5):48-51.
Chemical structure of a series of nitrophenols and their derivatives was studied in relation to their toxicity and complex-formation ability (association constant, amount of binding sites) with human blood serum albumin. Five compounds were studied using equilibrium dialysis and spectrofluorimetry. The nitrophenols, containing a hydrocarbon radical, exhibited distinctly higher affinity to albumin; substitution of one or two nitrogroups by aminogroups led to complete loss of the affinity to the protein. Dependence of acute toxicity on association constants of the complexes is discussed.
研究了一系列硝基苯酚及其衍生物的化学结构与其毒性以及与人血清白蛋白形成复合物的能力（缔合常数、结合位点数量）之间的关系。使用平衡透析和荧光光谱法对五种化合物进行了研究。含有烃基的硝基苯酚对白蛋白表现出明显更高的亲和力；一个或两个硝基被氨基取代导致对蛋白质的亲和力完全丧失。讨论了急性毒性对复合物缔合常数的依赖性。
