Triton X-100与牛血清白蛋白的相互作用

应用荧光光谱法研究了溶液体系中Ｔｒｉｔｏｎ Ｘ－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

The Interaction Between Triton X-100 and Bovine Serum Albumin

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.