Thorn W, Weiland E, Wasmus G
Res Exp Med (Berl). 1979 May 30;175(2):155-8. doi: 10.1007/BF01851822.
Nine glycoprotein-protein fractions prepared of erythropoietin-active crude urinary protein and separated by gel filtration on Sephadex G-50, ion exchange chromatography on Sephadex DEAE A-50, gel filtration on Sephacryl S-200 and Sepharose 6B were investigated by analytical isotachophoresis. 7 to 38 components could be separated of every chromatographic fraction investigated using chloride as leading and glycinate as terminating electrolyte. Improvement of resolution is possible by variation of buffer system conditions.
对从具有促红细胞生成素活性的粗制尿蛋白中制备的9种糖蛋白-蛋白质级分进行了研究，这些级分通过在Sephadex G-50上进行凝胶过滤、在Sephadex DEAE A-50上进行离子交换色谱、在Sephacryl S-200和Sepharose 6B上进行凝胶过滤来分离，采用分析等速电泳法进行研究。以氯化物作为先导电解质、甘氨酸盐作为终止电解质，对所研究的每个色谱级分可分离出7至38个组分。通过改变缓冲系统条件有可能提高分离度。
