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.
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