Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2089260 | Journal of Immunological Methods | 2006 | 7 Pages |
Abstract
Moraxella catarrhalis IgD-binding protein (MID) is a multimeric outer membrane protein belonging to the family of autotransporters. The IgD-binding domain of MID is located between amino acids MID 962-1200 and binds to amino acids 198-224 of the IgD CH1 region. In the present study, we describe a method to purify IgD from serum with high levels of IgD using a two-step affinity chromatography process. The first step involves depletion of MID-specific antibodies of all classes from serum using the non-IgD-binding fragment MID1000-1200. This step is followed by selective capture of IgD with MID962-1200. Furthermore, we demonstrate that the eluted IgD is pure, intact and functional for use in downstream applications. Our approach reduces the non-specificity commonly associated with lectin-based IgD purification regimes that rely on glycosylation of the IgD molecule.
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Authors
Martin Samuelsson, Arne Forsgren, Kristian Riesbeck,