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机构地区:[1]浙江师范大学化学与生命科学学院 [2]金华广播电视大学,浙江金华321000
出 处:《浙江师范大学学报(自然科学版)》2005年第4期407-412,共6页Journal of Zhejiang Normal University:Natural Sciences
基 金:浙江省自然科学基金资助项目(Y404031)
摘 要:采用荧光光谱法和吸收光谱法研究了1-(2-吡啶偶氮)-2-萘酚-磺酸(PAN-S)与牛血清白蛋白(BSA)的结合反应.研究表明,PAN-S对BSA的荧光猝灭机理为静态猝灭.测定了反应的结合常数(K=5.32×105~8.53×105L·mol-1)、荧光猝灭常数(Ksv=7.08×105L·mol-1)及结合位点数(n=2.88).进一步通过同步荧光法研究了PAN-S对BSA构象的影响,认为PAN-S主要结合在BSA的色氨酸残基附近.研究发现,PAN-S与BSA之间存在着类似于其同阳离子表面活性剂的静电作用.The binding reaction between 1-(2-pyridylazo)-2-naphthol-sulfonic acid (PAN-S) and bovine serum albumin(BSA) was studied by using fluorescence spectra and absorption spectra. The fluorescence spectra showed the quenching mechanism of BSA by PAN-S was a static quenching mechanism. The results showed that the binding constant K was 5.32×10^5~8.53×10^5L·mol^-1 , the quenching constant Ksv was 7.08×10^5L·mol^-1 , the number of binding sited n=2.88. The effect of PAN-S on conformation of BSA was further analyzed by using synchronous fluorescence spectrometry. By further research it was found that there were hydrophobic interactions between PAN-S and BSA. Meanwhile similar to cationic surfactand, static electric interactions existed between PAN-S and BSA.
关 键 词:牛血清白蛋白 1-(2-吡啶偶氮)-2-萘酚-磺酸 荧光光谱 吸收光谱
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