Ni(Ⅱ)与HSA或BSA的结合平衡研究
Binding Equilibrium Study between Ni(Ⅱ) and HSA or BSA
作者单位
沈星灿 广西师范大学生物无机化学研究所·化学化工系, 桂林541004 
边贺东 广西师范大学生物无机化学研究所·化学化工系, 桂林541004 
涂楚桥 广西师范大学生物无机化学研究所·化学化工系, 桂林541004 
张宏志 广西师范大学生物无机化学研究所·化学化工系, 桂林541004 
梁宏 广西师范大学生物无机化学研究所·化学化工系, 桂林541004 
周永洽 南开大学化学系, 天津300071 
申泮文 南开大学化学系, 天津300071 
摘要: 用平衡透析法研究了生理pH(7.43)及pH(5.0)条件下Ni(Ⅱ)与HSA或BSA的结合平衡。Scatchard图分析表明,生理pH条件下,Ni(Ⅱ)在HSA或BSA中均有2个强结合部位,而在pH(5.0)条件下,只有1个强结合部位。Hill图分析表明Ni(Ⅱ)与HSA或BSA的结合均产生较强的正协同效应。通过不同pH对Ni(Ⅱ)与HSA或BSA结合的影响及Ni(Ⅱ)与Cu(Ⅱ)和Ca(Ⅱ)的竞争结合的结果,推测了两个强结合部位可能的结合位点和配位原子。竞争结果还表明Cu(Ⅱ)对Ni(Ⅱ)的结合有明显
关键词: Ni(Ⅱ)-血清白蛋白  平衡透析  协同效应  配位分析
基金项目: 国家自然科学基金(No.29961001);广西十百千人才基金;广西高校自然科学基金资助项目
Abstract: The binding of Ni(Ⅱ) to human serum albumin(HSA) or bovine serum albumin (BSA) has been studied by equilibrium dialysis at physiological pH(7.43)and pH(5.0). The Scatchard analysis indicates that there exists 2 strong binding sites of Ni(Ⅱ) in both HSA and BSA at physiological pH(7.43),but only 1 strong binding site in both systems at pH(5.0). The analyses of Hill plot indicate that there exists strong positive cooperative effect in these systems. The Nterminal are probably the together strong binding locations of Ni(Ⅱ) and Cu(Ⅱ),which suggested through competition between Ni(Ⅱ) and Cu2+、Ca2+ ions. It also suggested that Natoms are the main coordinated atoms. Cu2+ ions induced an antagonism effect on Ni(Ⅱ)-HSA and Ni(Ⅱ)-BSA systems, and Ca2+ ions have litter effect on Ni(Ⅱ) binding to HSA or BSA.
Keywords: Ni(Ⅱ)-serum albumin  equilibrium dialysis  cooperative effect  coordination analysis
投稿时间:1999-06-01 修订日期:1999-09-27
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沈星灿,边贺东,涂楚桥,张宏志,梁宏,周永洽,申泮文.Ni(Ⅱ)与HSA或BSA的结合平衡研究[J].无机化学学报,2000,16(1):73-78.
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