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运用荧光光谱法研究了锰(Ⅱ,M n2+)与牛血清白蛋白(Bovine Serum A lbumin,BSA)的相互作用。随着Mn2+浓度的增大,BSA的荧光强度降低,最大发射峰蓝移2nm,根据Stern-Volmer方程求出了M n2+与BSA作用的猝灭常数,其猝灭机制为静态猝灭。根据热力学方程求得了290K和308K时的热力学参数$H、$G和$S,结果表明温度升高M n2+与BSA的作用增强,二者之间的作用力主要为疏水作用和静电作用。
The interaction between manganese (Ⅱ, M n2 +) and bovine serum albumin (BSA) was studied by fluorescence spectroscopy. With the increase of Mn2 + concentration, the fluorescence intensity of BSA decreased and the maximum emission peak shifted blue by 2 nm. According to the Stern-Volmer equation, the quenching constant of the interaction between M n2 + and BSA was obtained. The quenching mechanism was static quenching. The thermodynamic parameters $ H, $ G and $ S at 290K and 308K were obtained according to the thermodynamic equation. The results show that the effect of temperature increase on M n2 + and BSA is enhanced. The interaction between the two is mainly hydrophobic and electrostatic.