【摘要】 研究了尼古丁对牛血清蛋白荧光光谱变化,以及牛血清蛋白荧光猝灭机制,同时利用同步荧光研究了尼古丁对酪氨酸和色氨酸的影响,结果表明:尼古丁猝灭牛血清蛋白荧光是通过静态机制,形成常数为KA=2.1×107 L.mol-1,每一个牛血清蛋白分子结合尼古丁的位点数为0.22,牛血清蛋白与尼古丁的这种结合是很弱的,没有影响分子的构象,酪氨酸残基荧光没有变化,只是色氨酸荧光强度降低,荧光峰位置不变。更多还原

【Abstract】 The fluorescence spectra was employed to study the interaction between nicotine and BSA,and we also studied the affecting of nicotine to Trp,Tyr residues by synchronous fluorescence.The results demonstrate that nicotine could quench the fluorescence of BSA by mechanism of static process rather than dynamic,the contant is KA= 2.1×107 L·mol-1,the binding sites number is 0.22.The synchronous fluorescence spectra of tyrosine residues did not demonstrate any change.But the intensity of tryptophane residues fluorescence was decreased.Suggesting that nicotine affect BSA fluorescence spectra though affecting tryptophane residues fluorescence.更多还原