Ehsani N, Nyström M
Laboratory of Technical Polymer Chemistry, Lappeenranta University of Technology, Finland.
Bioseparation. 1995 Feb;5(1):1-10.
Fractionation of the model proteins, bovine serum albumin and myoglobin, was studied with modified and unmodified polysulfone ultrafiltration membranes. A commercial polysulfone ultrafiltration membrane with a nominal cut-off value of 50,000 g mol-1 was used as the reference membrane, and it was modified with ultraviolet irradiation in different protein solutions. The permeate fluxes and the streaming potentials of the membranes were measured simultaneously. Ultrafiltration experiments were carried out at the isoelectric points of the proteins. The results show that the fractionation can best be carried out at the isoelectric point of myoglobin. Modification of the membranes with bovine serum albumin resulted in smaller adsorption and flux reduction, while membranes modified with myoglobin were more selective for myoglobin.
使用改性和未改性的聚砜超滤膜对模型蛋白牛血清白蛋白和肌红蛋白进行了分级分离研究。将标称截留值为50,000 g mol-1的商用聚砜超滤膜用作参考膜，并在不同的蛋白质溶液中用紫外线照射对其进行改性。同时测量了膜的渗透通量和流动电位。超滤实验在蛋白质的等电点进行。结果表明，分级分离在肌红蛋白的等电点进行效果最佳。用牛血清白蛋白对膜进行改性导致吸附和通量降低较小，而用肌红蛋白改性的膜对肌红蛋白更具选择性。
