Isoprotein analysis by ion-exchange chromatography using a linear pH gradient combined with a salt gradient

Isoproteins of human monoclonal antibodies with a p I range between 8.45 and 8.70 or 8.15 and 8.65 were separated by ion-exchange chromatography with a linear ascending pH gradient combined with a linear descending salt gradient using borax, mannitol and salt. The isoproteins were eluted according t...

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Bibliographic Details
Published in:Journal of Chromatography A 1993-06, Vol.639 (1), p.41-49
Main Authors: Kaltenbrunner, O., Tauer, C., Brunner, J., Jungbauer, A.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Glycoproteins
Proteins
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Summary:Isoproteins of human monoclonal antibodies with a p I range between 8.45 and 8.70 or 8.15 and 8.65 were separated by ion-exchange chromatography with a linear ascending pH gradient combined with a linear descending salt gradient using borax, mannitol and salt. The isoproteins were eluted according to their isoelectric points as demonstrated by conventional isoelectric focusing. Preparative purification and monitoring of the isoprotein composition of human monoclonal antibodies during a purification process is also presented to demonstrate the applicability of the method.
ISSN:0021-9673
DOI:10.1016/0021-9673(93)83086-8