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荧光光谱法研究桑色素与人血清白蛋白的相互作用
引用本文:赵文华,高军林. 荧光光谱法研究桑色素与人血清白蛋白的相互作用[J]. 福建分析测试, 2013, 0(6): 10-13
作者姓名:赵文华  高军林
作者单位:中山职业技术学院,广东中山528404
摘    要:采用荧光猝灭光谱、紫外-可见吸收光谱研究了桑色素与人血清白蛋白(HSA)的结合作用。实验表明桑色素对HSA的荧光猝灭属于单一静态猝灭反应,在溶液中以摩尔比1:1牢固结合,各结合反应的平衡常数Kp>105,结合常数Kb>104;根据F rster非辐射能量转移机理,求算HSA与桑色素间距离r为3.81~3.58nm,能量转移效率E为0.18~0.13。并根据结合反应的热力学常数推测了药物与HSA之间的主要作用力类型为疏水作用力和偶极-偶极作用力。

关 键 词:桑色素  人血清白蛋白  荧光猝灭

Study on the Interaction of Morin with Human Serum Albumin by Fluorescence Spectroscopic Methods
Zhao Wen-hua,Gao Jun-lin. Study on the Interaction of Morin with Human Serum Albumin by Fluorescence Spectroscopic Methods[J]. Fujian Anal Ysis & Testing, 2013, 0(6): 10-13
Authors:Zhao Wen-hua  Gao Jun-lin
Affiliation:(ZhongShan polytechnic college, Zhongshan,Guangdong 528404,China)
Abstract:The interaction of Morin with Human Serum Albumin (HSA) was studied by Spectrometry , UV- visible absorption spectrophotometry and fluorescence spectrometry. The result show that the Morin could induce an endogenous fluorseence quenching of HSA ,which was proved to be a process of static quenching by the fitting equations of Stern- Volmer and double logarithm equation. The binding constants were determined to be more than 104.The binding site (n) was about 1.The binding distance was estimated to be 3.81-3.58nm according to Ffirster nonradiation energy transfer mechanism.Energy transfer effciency of E were 0.18N0.13J.The thermodynamic parameters suggested that the interaction forces between Morin and HSA were mainly hydrophobic interaction and dipole-dipole interaction.
Keywords:Fluorescence quenching  Morin  human serum albumin (HSA)
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