Summary
Nine glycoprotein-protein fractions prepared of erythropoietinactive 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.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Alhadeff, J.-A.: Gel filtration of sialoglycoprotein. Biochem. J.173, 315–319 (1978)
Bier, M., Cuddeback, R. M., Kopwillem, A.: Preparative plasma protein fractionation by isotachophoresis in sephadex columns. J. Chromatogr.132, 437–450 (1977)
Cotes, P. M.: Assay and standardization of erythropoietin. Ann. New York Acad. Sci.149, 12–17 (1968)
Espada, J., Gutnisky, A.: A new method for concentration of erythropoietin from human urine. Biochem. Med.3, 315–319 (1978)
Puschmann, M., Thorn, W., Yen, Y.-C.: Partial purification procedure for human urinary erythropoietin by preparative isotachophoresis. Res. Exp. Med. (Berl.)173, 293–296 (1978)
Author information
Authors and Affiliations
Additional information
Support of this work by the Deutsche Forschungsgemeinschaft is gratefully acknowledged (Th 77/35)
Rights and permissions
About this article
Cite this article
Thorn, W., Weiland, E. & Wasmus, G. Investigation of a glycoprotein-protein mixture from urine of anemic patients by analytical isotachophoresis. Res. Exp. Med. 175, 155–158 (1979). https://doi.org/10.1007/BF01851822
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01851822