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

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 sim

SUBMITTER: Svoboda M 

PROVIDER: S-EPMC3320794 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature