Mn(Ⅱ)与BSA相互作用的热力学特征  

Thermochemical Characteristics on the Reaction of Manganese Ion with Bovine Serum Albumin

作　　者：荣先国[1] 高宗华[1] 黄玉玲[1] 张怀斌[1] 

机构地区：[1]滨州医学院(烟台校区)药学院,山东省烟台市观海路346号264003

出　　处：《光谱实验室》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)

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.

关 键 词：Mn2+ 牛血清白蛋白 荧光猝灭 热力学特征 

分 类 号：O657.32[理学—分析化学]