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基于共振光散射光谱(RLS)研究了牛血清白蛋白(BSA)与肝素(HP)之间的结合平衡。结果表明,HP与BSA通过电子作用力以及疏水作用力结合,引起体系共振光散射增强。根据406nm的光散射增强信号建立了BSA与HP结合平衡的数学关系式,并考察了不同温度、pH及离子强度对它们之间结合平衡的影响。基于RLS数据计算了BSA与HP在不同温度及pH条件下的表面结合常数、结合位点数及相互过程中的热力学参数。
Binding equilibrium between bovine serum albumin (BSA) and heparin (HP) was investigated based on Resonance Light Scattering Spectroscopy (RLS). The results show that HP and BSA combine electron force and hydrophobic force to cause the system to enhance the resonance light scattering. According to the light scattering enhancement signal at 406 nm, the mathematical relationship between BSA and HP binding equilibrium was established and the effects of different temperature, pH and ionic strength on the binding equilibrium between them were investigated. Based on the RLS data, the surface binding constants, binding sites and thermodynamic parameters of BSA and HP at different temperatures and pHs were calculated.