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用荧光光谱和紫外吸收光谱研究了pH =2 3～ 1 1 3范围内牛血清白蛋白 (BSA)芳香氨基酸残基微环境的变化 ,以此推断蛋白质构象的变化 ,并讨论蛋白质表面疏水性变化的趋势。与中性环境相比 ,pH为 2 3时 ,色氨酸微环境的疏水性增强 ,蛋白质局部表面疏水降低 ;pH为 1 1 3时 ,部分Phe残基微环境的极性增强 ,表明碱诱导蛋白质分子变性使蛋白质分子充分伸展 ,将更多疏水性氨基酸残基暴露于溶剂中。
The changes of microenvironment of aromatic amino acid residues in bovine serum albumin (BSA) in the range of pH = 23 ~ 1 13 were studied by fluorescence and ultraviolet absorption spectroscopy to deduce the changes of protein conformation and to discuss the changes of protein surface hydrophobicity the trend of. Compared with the neutral environment, the pH of the tryptophan microenvironment enhanced the hydrophobicity of the microenvironment and decreased the hydrophobicity of the local surface of the protein. At the pH of 11 3, the polarity of some Phe residues in the microenvironment increased, indicating that alkaline induction Protein denaturation fully stretches protein molecules and exposes more hydrophobic amino acid residues to the solvent.