【摘要】 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。更多还原

【Abstract】 The interaction of horse heart hemoglobin with Hypocrellin A（HA） was studied by means of （UV-Vis） absorption spectroscopy and fluorescence spectroscropy under physiological condition. In the UV-Vis absorption spectrum, the intensity of the absorption peak of amino acid residues in the hemoglobin molecule decreases and the peak shifts bathochromically due to the hydrogen bonding between the amino acid （residue） in the hemoglobin molecule and HA. The synchronous fluorescence spectra show that the degree of the interaction of HA with different amino acid residues are different. For example, the fluorescence quenching kinetic （constants） of HA for tryptophane and tyrosine residues were 5.510¹² and 1.710¹² L/mol, respectively, which clearly demonstrates that the interaction between HA and tryptophane residue is more intense than that between HA and tyrosine residue.更多还原