摘要
应用荧光光谱法研究了溶液体系中TritonX-100（TX）与牛血清白蛋白（BSA）之间的相互作用。实验表明TX对BSA的荧光有较强的猝灭作用，二者形成不发荧光的复合物所产生的静态猝灭是引起BSA荧光猝灭的主要原因。从荧光猝灭结果求得二者的结合常数，发现在不同TX浓度下，结合常数K及络合个数n均不同；低于TX的cmc，K=440mol／L，n=0．91，高于cmc，K=10mol／L，n＝0．42。疏水作用是TX与BSA相互结合的主要驱动力。
The binding of Triton X-100(TX) to bovine serum albumin (BSA) was studied using nuorescence spectroscopy.It was shown that TX has a strong ability to quench the BSA fluorescence mainly via a static openching.The binding constant K and the number of bindig n were obtained from the fluorescene quenching results.It was revealed that K and n were changed with varying concertraions of TX: below cmc of TX, K was 440 mol/L, n was 0.91; above cmc, K was 10 mg/L, n was 0.42.The hydrophobic interactions played a major role in the binding process.
出处
《分析化学》
SCIE
EI
CAS
CSCD
北大核心
2000年第6期699-701,共3页
Chinese Journal of Analytical Chemistry
基金
国家自然科学基金
