Naik D V, Paul W L, Schulman S G
J Pharm Sci. 1975 Oct;64(10):1677-80. doi: 10.1002/jps.2600641020.
The binding of pamaquine to bovine serum albumin is accompanied by the enhancement of the fluorescence efficiency of the former but without shifting its fluorescence energy. This phenomenon was used to evaluate the stoichiometry and strength of the binding. The results indicate that three singly protonated pamaquine molecules are bound by each bovine serum albumine molecule. The individual binding constants were calculated by using the Bjerrum technique. The average values of the three constants were K1 = 6.4 X 10(7), K2 = 3.1 X 10(6), and K3 = 1.9 X 10(5), indicating that, compared to anionic drugs and fluorescent probes, pamaquine is very strongly bound by the protein.
伯氨喹与牛血清白蛋白结合时，前者的荧光效率增强，但荧光能量未发生偏移。利用这一现象评估结合的化学计量和强度。结果表明，每个牛血清白蛋白分子结合三个单质子化的伯氨喹分子。采用比耶鲁姆技术计算各个结合常数。这三个常数的平均值分别为K1 = 6.4×10⁷、K2 = 3.1×10⁶和K3 = 1.9×10⁵，表明与阴离子药物和荧光探针相比，伯氨喹与该蛋白质的结合非常紧密。
