Pb^(2+)与HSA或BSA的结合平衡研究  

Study on binding equilibrium between Pb^(2+) and HSA or BSA

作　　者：王改珍[1] 苗凤智[1] 程艳坤[1] 薛瑞[1] 张晶[1] 崔艳[1] 孟宪竟[1] 

机构地区：[1]河北科技大学环境科学与工程学院,河北石家庄050018

出　　处：《河北科技大学学报》2009年第4期310-313,共4页Journal of Hebei University of Science and Technology

基　　金：河北省自然科学基金资助项目(B2006000308)

摘　　要：用平衡透析法详细研究了模拟生理pH值为6.3条件下,Pb^(2+)与人血清白蛋白(HSA)或牛血清白蛋白(BSA)的结合平衡。Scatchard图分析表明,Pb^(2+)在BSA和HSA中分别有1.6和1.8个强结合位点,通过非线性最小二乘法拟合Bjerrum方程,得到了Pb^(2+)-HSA体系和Pb^(2+)-BSA体系的逐级稳定常数,其中K_1,K_2均明显大于其余K值。Hill系数分析表明,Pb^(2+)与HSA或BSA的结合存在弱负协同效应。The binding of Pb^2＋ to human serum albumin（HSA） or bovine serum albumin （BSA） has been studied by equilibrium dialysis at pH 6.3. Scatchard analysis indicates that there are 1.6 and 1.8 strong binding sites for Pb^2＋ in BSA and HSA, respectively. The successive stability constants for the Pb^2＋-HSA and Pb^2＋-BSA systems are determined by non-linear leastsquare method fitting Bjerrum formula. Of these stability constants, K2 and K2 are obviously higher than the values of the other stability constants. The analysis of Hill plot indicates that there exists weak negative cooperative effect in both Pb^2＋-HSA and Pb^2＋-BSA systems.

关 键 词：铅离子 血清白蛋白 平衡透析 协同效应 

分 类 号：O629.73[理学—有机化学]