摘要
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 mechanism of manganese ion （ Ⅱ ,Mn^2＋） and bovine serum albumin （BSA） was studied by the fluorescence spectroscopy. The fluorescence spectroscopy of BSA quenched with adding the concentration of Mn^2＋. The maximum emission wavelength of BSA was blueshift 2nm. On the basis of Stern-Volmer equation,the quenching constant was obtained,and the quenching mechanism of BSA was a static quenching machenism. Judging by relevant thermodynamics formula, the thermodynamic parameters （△H, AG and △S） were calculated. The results suggested that the conjugation＇ of Mn^2＋ and BSA enhanced with elevating the tempreture and the acting force was mainly hydrophobic force and electrostatic interaction.
出处
《光谱实验室》
CAS
2013年第6期3130-3133,共4页
Chinese Journal of Spectroscopy Laboratory
基金
山东省高等学校科技计划资助项目(J12LD55)
滨州医学院科研专项资助项目(BY2009KJ30)
关键词
Mn2+
牛血清白蛋白
荧光猝灭
热力学特征
Manganese Ion
Bovine Serum Albumin
Fluorescence Quenching
ThermodynamicCharacteristics
