引用本文:
宁爱民, 党玉丽, 赵士举, 宛新生, 郑先福. 电动势法研究蛋白质与季铵盐Gemini表面活性剂的相互作用[J]. 应用化学,
2011, 28(7): 826-830.
doi:
10.3724/SP.J.1095.2011.00534
Citation: NING Aimin, DANG Yuli, ZHAO Shiju, WAN Xinsheng, ZHENG Xianfu. Study on the Interaction of Protein with Quaternaryammonium Gemini Surfactants by Electromotive Force Method[J]. Chinese Journal of Applied Chemistry, 2011, 28(7): 826-830. doi: 10.3724/SP.J.1095.2011.00534
Citation: NING Aimin, DANG Yuli, ZHAO Shiju, WAN Xinsheng, ZHENG Xianfu. Study on the Interaction of Protein with Quaternaryammonium Gemini Surfactants by Electromotive Force Method[J]. Chinese Journal of Applied Chemistry, 2011, 28(7): 826-830. doi: 10.3724/SP.J.1095.2011.00534
电动势法研究蛋白质与季铵盐Gemini表面活性剂的相互作用
摘要:
利用自制的季铵盐Gemini表面活性剂二溴化-N,N'-二(二甲基十二烷基)丙二铵(C12-3-C12·2Br)离子选择电极,通过电动势(EMF)法研究了C12-3-C12·2Br与牛血清白蛋白(BSA)之间的相互作用,得到了C12-3-C12·2Br在BSA大分子上结合过程的结合等温线和对应的Scatchard曲线,并通过结合能力的概念得到了结合过程的结合位点数、Hill系数及Hill结合常数。通过研究发现,C12-3-C12·2Br与BSA大分子的结合具有正的协同作用,相互结合的位点可以分为两类,第一类为主要通过静电作用结合的强结合位点,第二类为主要通过疏水作用结合的弱结合位点。
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关键词:
- 季铵盐Gemini表面活性剂
- / 电动势
- / 牛血清白蛋白
- / 结合等温线
- / 结合能力
English
Study on the Interaction of Protein with Quaternaryammonium Gemini Surfactants by Electromotive Force Method
Abstract:
An ion selective electrode of quaternary-ammonium gemini surfactant C12-3-C12·2Br has been fabricated.The variation of electromotive force(EMF) of the systems of C12-3-C12·2Br and bovine serum albumin(BSA) with the concentration of C12-3-C12·2Br has been studied.The binding isotherms and Scatchard plots of the interaction of C12-3-C12·2Br with BSA molecules have been obtained.The numbers of binding sites,Hill coefficient and Hill binding constant have been calculated on the basis of the binding capacity.The results show that the interaction of C12-3-C12·2Br with BSA molecules behaved a positive cooperativity in the binding process.There are two types of binding sites on BSA for C12-3-C12·2Br.One is high-affinity binding site at which the essential role of the interaction is electrostatic force,and the other is low-affinity binding site at which the essential role of interaction is hydrophobic force.
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