Light scattering study of complex formation between protein and polyelectrolyte at various ionic strengths
Light scattering study of complex formation between protein and polyelectrolyte at various ionic strengths
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DOI：
10.1016/j.colsurfb.2006.10.003
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发表时间：
2007-04-15
影响因子：
5.8
通讯作者：
Kokufuta, Etsuo
中科院分区：
文献类型：
--
作者：
Matsunami, Hiroshi;Kikuchi, Rie;Kokufuta, Etsuo
研究了pH = 3时，聚乙烯醇硫酸钾（KPVS）与牛血清白蛋白（BSA）形成蛋白质-淀粉复合物（PPC）的离子强度的变化。采用动态光散射（DLS）和电泳光散射（ELS）相结合的浊度滴定法。通过假设自由排水和非自由排水模型，从ELS数据估计得到的PPC在不同离子强度下的形式电荷（Z（ppc））。在前一种模型中，复合物中BSA分子的半径用于用亨利方程计算Zppc，而在后一种情况下，采用从DLS确定的PPC颗粒的流体动力学半径。将获得的结果与使用Z（ppC）= n（B）Z（BSA）+ alpha Z（KPVS）的关系计算的Z（ppC）值进行比较，其中Z（BSA）（>= 0）和Z（KPVSW）（
Formation of protein-polyelectrolyte complexes (PPCs) between bovine serum albumin (BSA) and potassium poly (vinyl alcohol) sulfate (KPVS) was studied at pH 3 as a function of ionic strength. Turbidimetric titration was employed by a combination of dynamic light scattering (DLS) and electrophoretic light scattering (ELS). The formal charge (Z(ppc)) of the resulting PPCs at different ionic strengths were estimated from ELS data by assuming the free draining and the non-free draining model. The radius of a BSA molecule in the complex was used in the former model for calculation of Zppc with the Henry's equation, while in the latter case the hydrodynamic radius of a PPC particle determined from DLS was employed. The results obtained were compared with the Z(ppC) values calculated using a relation of Z(ppC) = n(b)Z(BSA) + alpha Z(KPVS), where Z(BSA) (>= 0) and Z(KPVSW) (