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利用UV-Vis吸收光谱和荧光光谱研究了在生理pH值条件下竹红菌甲素(HA)与血红蛋白的相互作用。UV-Vis吸收光谱的研究发现,HA的存在使血红蛋白分子中氨基酸残基的吸收峰强度降低,峰位红移,表明HA与血红蛋白分子中的氨基酸残基形成氢键。同步荧光光谱的结果表明,HA与血红素分子中不同氨基酸残基的作用强度不同,HA对色氨酸残基和酪氨酸残基的荧光猝灭动力学常数分别为5.5×1012和1.7×1012L/mol,表明HA与色氨酸残基之间的相互作用强于与酪氨酸残基。
UV-Vis absorption spectra and fluorescence spectra were used to study the interaction between hypocrellin A (HA) and hemoglobin at physiological pH. UV-Vis absorption spectrum studies have found that the presence of HA reduces the intensity of the absorption peaks of amino acid residues in the hemoglobin molecule and red shifts the peak positions, indicating that HA forms hydrogen bonds with amino acid residues in the hemoglobin molecule. The results of synchronous fluorescence spectroscopy show that the different intensity of different amino acid residues in HA and heme molecules is different, and the fluorescence quenching constants of tryptophan and tyrosine residues in HA are 5.5×1012 and 1.7× respectively. 1012 L/mol, indicating that the interaction between HA and tryptophan residues is stronger than with tyrosine residues.