人血清蛋白和血栓烷A_2合成酶抑制剂的相互作用

本文研究了血栓烷A_2合成酶抑制剂OKY—1580和OKY—046与人血清蛋白的相互作用,测定了结合强度,判定了结合部位,并将平衡透析法所得数据用Scatchard法画图决定了结合参数。人血清蛋白分子内赖氨酸—199残基和色氨酸—214残基近旁(U部位)同三硝基苯磺酸与5—硝基乙酰水杨酸的反应被OKY—1580所抑制。OKY—1580结合人血清蛋白减弱了人血清蛋白分子内色氨酸—214残基的荧光强度。可见,OKY—1580与人血清蛋白结合部位为U部位。

Interaction between Human Serum Albumin and Thromboxane A_2 Synthetase Inhibitor

The interactions of OKY-1580 and OKY-046 with human serum albumin(HSA), the bindin affinity and the binding sites were studied. The binding parameters were determined by the scatchard plots using the equilibrium dialysis data. The binding power of OKY-1580 to HSA was about 35-fold stronger than that of OKY-046. The reaction of trinitrobezene sulfonates and 5-nitroaspirin with HSA, which occured near lysin-199 and tryptophan-214 residues (U site) in the HSA, was slightly inhibited by OKY-1580. The fluorecence intensity of the tryptopban-214 residue was decreased by combinding the OKY-1580 with HSA, which indicated the binding position was U site.