光谱法研究十二烷基苯磺酸钠与牛血清白蛋白的相互作用

在pH=7.40的Tris-HCl缓冲溶液体系中,通过荧光光谱法研究了十二烷基苯磺酸钠与牛血清白蛋白的相互作用。运用Stern-Volmer方程和Lineweaver-Burk方程计算了其相互间的猝灭常数、结合常数及结合位点数,在298,308和318K时的表观结合常数分别为0.4108,0.3605和0.048 98 L.μmol-1,其相应的结合位点数分别为1.044,1.041和0.9026,利用热力学参数确定了分子间的作用过程是自发的,作用力主要是静电作用力。同步荧光光谱表明相互作用对蛋白质构象影响不大。

Study of mutual action between bovine serum albumin and sodium dodecyl benzene sulfonate by spectrometry

Mutual action between sodium dodecyl benzene sulfonate(SDBS) and bovine serum albumin(BSA) was investigated via fluorescence spectroscopy in a buffer solution composed of H2NC(CH2OH)3·HCl at pH=7.40.Their mutual quenching constants(Kq),apparent binding constants(KA),and binding site values(n) were calculated by using Stern-Volmer Equation and Lineweaver-Burk Equation.The apparent binding constants between SDBS and BSA at temperature of 298,308 and 318 K were obtained as 0.410 8,0.360 5 and 0.048 98 L·μmol-1 respectively;and the corresponding binding site values were 1.044,1.041 and 0.902 6 respectively.Analysis of thermodynamic parameters showed that the action process between the molecules is carried out spontaneously;and the action was caused by electrostatic force.Synchronous fluorescence spectra showed that the mutual action has no effect on the conformation of the protein molecules.