Hasegawa J, Nakayama T, Nozaki M, Fujimura H
Nihon Yakurigaku Zasshi. 1984 Jan;83(1):85-91.
The serum albumin-interaction of suprofen (SPF), a novel anti-inflammatory drug, was compared with those of indomethacin (IM) and ketoprofen (KTP). The binding constants of these drugs were determined with difference absorption spectra based on the binding to bovine serum albumin (BSA). The constants for SPF and IM were nearly equal, and the value for KTP was smaller than those of the other drugs. The magnitude of the inhibitory effect on heat denaturation of BSA reflected the difference in these binding constants. In the presence of these drugs, the tryptophan fluorescence in BSA was quenched (IM, SPF and KTP, in this order). The metachromagy based on the binding of an azodye, HABA, to BSA was potentiated by IM or SPF. Phenylbutazone suppressed the absorption of the metachromagy. SPF displaced only the binding of the fluorescent Site II probe, dansylproline, to human serum albumin (HSA), and both the bindings of dansylproline and dansylamide (Site I probe) to HSA were inhibited by KTP or IM. KTP released bilirubin from BSA and HSA, but SPF and IM did not show any effects on the bilirubin-serum albumin binding. These results all support that there is considerable interaction between SPF and serum albumin and that the mode of the interaction differs from those of KTP and phenylbutazone.
将新型抗炎药舒洛芬（SPF）与吲哚美辛（IM）和酮洛芬（KTP）的血清白蛋白相互作用进行了比较。基于这些药物与牛血清白蛋白（BSA）的结合，利用差示吸收光谱法测定了它们的结合常数。SPF和IM的常数几乎相等，而KTP的值小于其他药物。对BSA热变性的抑制作用大小反映了这些结合常数的差异。在这些药物存在下，BSA中的色氨酸荧光被淬灭（顺序为IM、SPF和KTP）。基于偶氮染料HABA与BSA结合的变色效应被IM或SPF增强。保泰松抑制了变色效应的吸收。SPF仅取代了荧光位点II探针丹磺酰脯氨酸与人血清白蛋白（HSA）的结合，而丹磺酰脯氨酸和丹磺酰胺（位点I探针）与HSA的结合均被KTP或IM抑制。KTP从BSA和HSA中释放胆红素，但SPF和IM对胆红素 - 血清白蛋白结合没有任何影响。这些结果均支持SPF与血清白蛋白之间存在相当大的相互作用，且相互作用模式与KTP和保泰松不同。
