Minami T, Price W S, Cutler D J
Department of Pharmacy, University of Sydney, New South Wales, Australia.
J Pharm Sci. 1992 May;81(5):419-23. doi: 10.1002/jps.2600810505.
Chloride-37 nuclear magnetic resonance spectroscopy was used to investigate the displacement of chloride (Cl-) from binding sites on band 3 anion transport protein in human erythrocytes by salicylic acid and five other hydroxybenzoic acids (HAs). All the HAs studied displaced Cl- from these binding sites. The association constants for binding of the HAs to band 3 anion transport protein were larger than that for Cl- and dependent on the specific structural features of the molecule, rather than general physicochemical characteristics.
利用氯-37核磁共振光谱研究了水杨酸和其他五种羟基苯甲酸(HAs)对人红细胞带3阴离子转运蛋白结合位点上氯离子(Cl-)的置换作用。所有研究的羟基苯甲酸都能从这些结合位点置换出Cl-。羟基苯甲酸与带3阴离子转运蛋白结合的缔合常数大于Cl-的缔合常数,且取决于分子的特定结构特征,而非一般的物理化学特性。