Affinity purification of IdeZ digest for Glycosylation profile of Immunoglobulins using a linear benchtop MALDI-TOFMS.

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.

Content Type:
Poster
Document Number:
PO-CON1852E
Product Type:
Keywords:
IdeZ, glycostation, MALDI-TOFMS, affinity purification, immunoglobins, Pharma & Biopharma, Monoclonal Antibodies and Biosimilars, MALDI-8020
Language:
English
File Name:
Shimadzu-jpo319079.pdf
File Size:
714kb

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For Research Use Only. Not for use in diagnostic procedures.

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