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目的:通过对稀土钐离子(Sm3+)和人血清白蛋白(HSA)的结合反应研究,进一步探讨Sm3+在生物体内与蛋白质相互作用的机理。方法:用荧光光谱、紫外-可见吸收光谱法研究了稀土金属离子与人血清白蛋白的相互作用。结果:Sm3+对HSA有荧光猝灭作用,属于静态猝灭,Sm3+与HSA反应生成了新的复合物,荧光猝灭发生了分子内的非辐射能量转移。Sm3+与HSA的结合常数Kb分别为4.12×105L.mol-1(298K)和2.26×105L.mol-1(318K),结合位点数n为1.24(298 K)和1.20(318 K)。结论:Sm3+和HSA之间有很强的结合作用,这为Sm3+在体内被蛋白质储存和转运提供了条件。
OBJECTIVE: To investigate the mechanism of the interaction between Sm3 + and protein in vivo through the binding reaction of Sm3 + with human serum albumin (HSA). Methods: The interaction between rare earth metal ions and human serum albumin was studied by fluorescence and UV-Vis absorption spectra. Results: Sm3 + had a fluorescence quenching effect on HSA, belonging to static quenching. Sm3 + reacted with HSA to form a new complex, and fluorescence quenching occurred intramolecular non-radiative energy transfer. The binding constants Kb between Sm3 + and HSA were 4.12 × 105L.mol-1 (298K) and 2.26 × 105L.mol-1 (318K), respectively. The number of binding sites n was 1.24 (298 K) and 1.20 (318 K). Conclusion: There is a strong binding between Sm3 + and HSA, which provides the conditions for the storage and transport of Sm3 + protein in vivo.