Peng G W, Chiou W L
Pharmacology. 1976;14(1):58-66. doi: 10.1159/000136580.
Protein binding of the aerosol propellant, trichloromonofluoromethane, was studied in bovine serum albumin (BSA) solutions using the fluorescent probe technique. The propellant displaced the probe, 8-anilino-1-naphthalenesulfonate, from its binding sites and reduced the fluorescence intensity. The binding association constants, the number of binding sites, and the competitive nature of the binding interaction were investigated. The hydrophobic nature of the binding and the implication of binding displacement interactions between the fluorocarbon and plasma-protein-bound drugs were also discussed. The fatty acid impurities present in the commercial BSA were found to have no effect on the protein binding of the propellant.
采用荧光探针技术，在牛血清白蛋白（BSA）溶液中研究了气雾剂推进剂三氯一氟甲烷的蛋白质结合情况。该推进剂将探针8-苯胺基-1-萘磺酸盐从其结合位点上置换出来，降低了荧光强度。研究了结合缔合常数、结合位点数量以及结合相互作用的竞争性质。还讨论了结合的疏水性质以及碳氟化合物与血浆蛋白结合药物之间结合置换相互作用的意义。发现市售BSA中存在的脂肪酸杂质对推进剂的蛋白质结合没有影响。
