论文部分内容阅读
在 0.1 mol?L-1醋酸-醋酸钠(pH 5.0)体系中, 采用紫外吸收光谱、荧光光谱及同步荧光光谱法研究了人血丙种球蛋白(gamma seroglobulinum humanum, 简称 GSH)与铱(IV)离子的相互作用. 结果表明, Ir(IV)离子使人血丙种球蛋白的构象发生了改变, α-螺旋含量减少, 并且用同步荧光光谱发现 Ir(IV)离子与人血丙种球蛋白的作用位点更接近于色氨酸,从而使色氨酸残基的疏水性略有减小. 荧光光谱结果表明Ir(IV)对人血丙种球蛋白内源荧光(342 nm)产生了较强的荧光猝灭作用, 根据不同温度下 Ir(IV)对人血丙种球蛋白的荧光猝灭作用, 证明了这种荧光猝灭为静态猝灭机制, 计算了其结合常数和结合位点数, 从而得出了静电作用力为其主要的作用力.
The effects of gamma seroglobulinum humanum (GSH) and iridium (IV) were studied by UV absorption spectroscopy, fluorescence spectroscopy and synchronous fluorescence spectrometry in a 0.1 mol? L-1 acetic acid-sodium acetate pH 5.0 system. Ion interaction.The results show that the Ir (IV) ion changes the conformation of human gamma globulin and decreases the alpha-helix content, and the effect of Ir (IV) ion on human gamma globulin is found by synchronous fluorescence spectroscopy Site closer to tryptophan, resulting in a slight decrease in hydrophobicity of the tryptophan residues.Fluorescence spectroscopy results showed that Ir (IV) produced a stronger endogenous fluorescence (342 nm) to human gamma globulin According to the fluorescence quenching of Ir (IV) on human blood gamma globulin at different temperatures, it is proved that this fluorescence quenching is a static quenching mechanism, and its binding constant and the number of binding sites are calculated, thus obtaining Out of the electrostatic force as its main force.