Examination of glycan profiles from IgG-depleted human immunoglobulins facilitated by microscale affinity chromatography.

Analytical Chemistry
Martin SvobodaMilos V Novotny

Abstract

Among the most important proteins involved in disease and healing processes are the immunoglobulins (Igs). Although many of the Igs have been studied through proteomics, aside from IgG, immunoglobulin carbohydrates have not been extensively characterized in different states of health. It seems valuable to develop techniques that permit an understanding of changes in the structures and abundances of Ig glycans in the context of disease onset and progression. We have devised a strategy for characterization of the glycans for the Ig classes other than IgG (i.e., A, D, E, and M) that contain kappa light chains that requires only a few microliters of biological material. First, we designed a microcolumn containing recombinant Protein L that was immobilized on macroporous silica particles. A similarly designed Protein G microcolumn was utilized to first perform an online depletion of the IgG from the sample, human blood serum, and thereby facilitate enrichment of the other Igs. Even though only 3 μL of serum was used in these analyses, we were able to recover a significantly enriched fraction of non-IgG immunoglobulins. The enrichment properties of the Protein L column were characterized using a highly sensitive label-free quantitati...Continue Reading

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Citations

Sep 5, 2012·Glycoconjugate Journal·Milos V NovotnyBenjamin F Mann
Mar 28, 2013·Chemical Reviews·William R AlleyMilos V Novotny
Jul 12, 2012·Glycobiology·Jacqueline A VasseurMilos V Novotny
Jun 25, 2013·Current Opinion in Chemical Biology·Milos V Novotny, William R Alley
Jan 21, 2017·Analytical Chemistry·Stefan GaunitzMilos V Novotny

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