L-半胱氨酸与牛血清白蛋白相互作用的荧光光谱分析  

Fluorescence Spectrometric Analysis on the Interaction between L-Cysteine and Bovine Serum Albumin

作　　者：徐大玮[1] 毕玉琦[2] 

机构地区：[1]山东省产品质量监督检验研究院,山东济南250100 [2]山东质量认证中心,山东济南250014

出　　处：《化学与生物工程》2013年第8期57-60,共4页Chemistry & Bioengineering

摘　　要：运用荧光猝灭光谱、同步荧光光谱探讨了L-半胱氨酸(L-Cys)与牛血清白蛋白(BSA)的相互作用,并计算了猝灭常数、结合常数、结合位点数以及3个热力学参数△H、△G和△S。结果表明,L-Cys使BSA的内源荧光发生猝灭,BSA的发射峰从350nm蓝移到347.5nm,荧光猝灭机制为动态猝灭;L-Cys与BSA之间的作用力主要为疏水作用力;L-Cys对BSA结构的微环境有一定的影响。The interaction between L-cysteine（L-Cys） and bovine serum albumin（BSA） was investigated by fluorescence quenching spectrum and synchronous fluorescence spectrum. The quenching constant, binding constant,binding sites of L-Cys with BSA, and the thermodynamic parameters （△H, △G,△S） were calculated. The fluorescence of BSA was quenched by L-Cys. The fluorescence peak of BSA shifted from 350 nm to 347.5 nm. Its quenching mechanism was a dynamic process. Their interaction force was hydrophobic force. The synchronous fluorescence spectrum showed that L-Cys influenced the mieroenvironment around BSA.

关 键 词：L-半胱氨酸 牛血清白蛋白 荧光猝灭光谱 同步荧光光谱 热力学参数 

分 类 号：O657.3[理学—分析化学]