Piasecki E, Inglot A D, Czyrski J A, Szulc Z, Młochowski J, Narczewska B
Arch Immunol Ther Exp (Warsz). 1985;33(2):299-310.
Equilibrium dialysis, gel filtration and SDS polyacrylamide gel electrophoresis were used to study the interaction of sodium salt of 9-oxo-10-acridineacetic acid (CMA) as well as its analogs 7, 8, 11, 13 - 16 with proteins. The compounds were found to bind mainly to serum albumins. Several other proteins had no affinity to the compounds. The close analogs 7 and 8 (sodium salt of 2,7-dibromo-9-oxo-10-acridineacetic acid and sodium salt of 9-oxo-10-acridinebutyric acid) which were inactive as interferon inducers were found to have greater affinity to bovine, mouse or human albumin than the active IFN inducer--CMA. The mechanism of interaction of CMA as well as its close analogs with albumin resembled the first phase of reaction of pharmacologically active ligands with their specific receptor or acceptor proteins. CMA and some of its close analogs were also shown to stabilize the human erythrocyte membrane against hemolysis in the hypotonic solution. However, the activity of the compounds was much weaker than that of other so called membrane active drugs.
采用平衡透析、凝胶过滤和SDS聚丙烯酰胺凝胶电泳法研究了9-氧代-10-吖啶乙酸（CMA）钠盐及其类似物7、8、11、13 - 16与蛋白质的相互作用。发现这些化合物主要与血清白蛋白结合。其他几种蛋白质对这些化合物没有亲和力。作为干扰素诱导剂无活性的紧密类似物7和8（2,7-二溴-9-氧代-10-吖啶乙酸钠盐和9-氧代-10-吖啶丁酸钠盐）被发现对牛、小鼠或人白蛋白的亲和力高于活性IFN诱导剂——CMA。CMA及其紧密类似物与白蛋白的相互作用机制类似于药理活性配体与其特异性受体或受体蛋白反应的第一阶段。还显示CMA及其一些紧密类似物可稳定人红细胞膜，使其在低渗溶液中不发生溶血。然而，这些化合物的活性比其他所谓的膜活性药物弱得多。
