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J Chromatogr A. 2007 Mar 9;1144(1):120-5. Epub 2006 Dec 20.

Fast and efficient separation of immunoglobulin M from immunoglobulin G using short monolithic columns.

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BIA Separations d.o.o., Teslova 30, SI-1000 Ljubljana, Slovenia.


Certain diagnostic, analytical and preparative applications require the separation of immunoglobulin G (IgG) from immunoglobulin M (IgM). In the present work, different ion-exchange methacrylate monoliths were tested for the separation of IgG and IgM. The strong anion-exchange column had the highest dynamic binding capacity reaching more than 20mg of IgM/ml of support. Additionally, separation of IgM from human serum albumin, a common contaminant in immunoglobulin purification, was achieved on the weak ethylenediamino anion-exchange column, which set the basis for the IgM purification method developed on convective interaction media (CIM) supports. Experiments also confirmed flow independent characteristics of the short monolithic columns.

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