Skidmore G L, Chase H A
Department of Chemical Engineering, University of Cambridge, U.K.
J Chromatogr. 1990 May 4;505(2):329-47. doi: 10.1016/s0021-9673(01)93048-1.
A model system, consisting of bovine serum albumin, lysozyme and the cation exchanger S Sepharose FF, was used to investigate multicomponent protein adsorption to ion exchangers. Two models, one based on a complete absence of competition between adsorbing molecules and the other a competitive model, based on the assumption that all adsorption sites are available to both proteins, have been compared to experimental results. Evidence for competitive adsorption was seen in experiments in which breakthrough curves and the profiles of adsorbed proteins in packed beds were determined. However, although the results for packed-bed experiments were more closely predicted by the fully competitive model, some discrepancies were found suggesting that when considering multicomponent protein adsorption to ion exchangers it may also be necessary to take account of factors such as the molecular size of the adsorbing proteins and any potential inter-protein interactions, factors which may hinder the development of a general model of multicomponent protein adsorption to ion exchangers.
一个由牛血清白蛋白、溶菌酶和阳离子交换剂S Sepharose FF组成的模型系统，被用于研究多组分蛋白质在离子交换剂上的吸附。基于吸附分子之间完全不存在竞争的一个模型和基于所有吸附位点对两种蛋白质均可用这一假设的竞争模型，已与实验结果进行了比较。在测定穿透曲线和填充床中吸附蛋白质的分布曲线的实验中发现了竞争吸附的证据。然而，尽管填充床实验的结果由完全竞争模型预测得更为准确，但仍发现了一些差异，这表明在考虑多组分蛋白质在离子交换剂上的吸附时，可能还需要考虑诸如吸附蛋白质的分子大小以及任何潜在的蛋白质间相互作用等因素，这些因素可能会阻碍多组分蛋白质在离子交换剂上吸附的通用模型的建立。
