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采用荧光光谱法研究了番茄红素(Lycopene)与牛血清白蛋白(BSA)的相互作用关系。研究表明,番茄红素能使BSA在340nm(λem)处产生荧光猝灭,猝灭机理为静态猝灭。pH=7.4,温度为293K时,猝灭时表观结合常数KA为5.33×104L.mol-1,结合位点数n为0.6461,同时荧光猝灭最大速率常数Kq=2.76×1012L.mol-1.s-1。二者呈自发结合且主要作用力为氢键和范德华力,结合距离r与能量转移效率E分别为5.6nm和0.098,偏酸性或碱性的条件使番茄红素与BSA的结合常数增加。
The interaction between lycopene and bovine serum albumin (BSA) was studied by fluorescence spectroscopy. Studies have shown that lycopene can make BSA fluorescence quenching at 340nm (λem), the quenching mechanism of static quenching. The apparent binding constant (KA) at quenching was 5.33 × 104 L · mol-1, the number of binding sites was 0.6461 at pH = 7.4 and 293 K, and the maximum rate constant of fluorescence quenching was Kq = 2.76 × 1012 L · mol-1. s-1. The two were spontaneous binding and the main force for the hydrogen bond and van der Waals forces, the binding distance r and energy transfer efficiency E were 5.6nm and 0.098, acidic or alkaline conditions make the binding constant of lycopene and BSA increased.