Buko V U, Zavodnik I B, Stepuro I I
Biokhimiia. 1987 Jun;52(6):891-5.
Using equilibrium dialysis, protein fluorescence and fluorescent probing as well as chemical modification, the interaction of prostaglandin E2 with human serum albumin was studied. The serum albumin molecule has a highly specific prostaglandin E2-binding site. The binding of prostaglandin causes conformational rearrangements in the protein molecule. The amino group of serum albumin is involved in the interaction with prostaglandin E2. Prolonged exposure of prostaglandin E2 to serum albumin causes partial irreversible binding of prostaglandin molecules to the protein.
采用平衡透析、蛋白质荧光和荧光探针以及化学修饰等方法,研究了前列腺素E2与人血清白蛋白的相互作用。血清白蛋白分子具有高度特异性的前列腺素E2结合位点。前列腺素的结合会导致蛋白质分子发生构象重排。血清白蛋白的氨基参与了与前列腺素E2的相互作用。前列腺素E2长时间暴露于血清白蛋白会导致前列腺素分子与蛋白质发生部分不可逆结合。