Glycosylation on protein plays wide-range vital roles in biological processes from stabilization of protein conformation to expression of binding specificity. In this view, a characterization of the N-/O-linked glycan is quite significant, especially, in development of biopharmaceuticals. To date, whereas intensive efforts were conducted to characterize glycans precisely with high-end mass spectrometers, conventional instruments without time consuming preparation has been anticipated for batch analysis in screening or QA/QC. A newly developed bench-top MALDI-TOFMS is expected to be the
conventional instrument in terms of sufficient specification, through-put, and cost effectiveness. We attempted to characterize glycosylation of IgG without a release of glycan using the bench-top MALDI-TOFMS. To do this, we examined a preparation using affinity beads and enzymatic cleavage.