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MAbs. 2013 Sep-Oct;5(5):641-5. doi: 10.4161/mabs.25302. Epub 2013 Jun 20.

Rapid Fc glycosylation analysis of Fc fusions with IdeS and liquid chromatography mass spectrometry.

Author information

1
GlycoFi; Biologics Discovery; Merck & Co. Inc.; Lebanon, NH USA.

Abstract

We developed a rapid method to analyze Fc glycosylation of Fc fusion proteins, especially those with mutated Fc hinge regions. Fc fusion proteins were digested with IdeS, an IgG specific protease with exosites for substrate recognition and cleavage. The resultant fragments were directly analyzed through liquid chromatography mass spectrometry. The structures and relative quantities of Fc glycans were deduced from their masses and intensities. The separated substrate recognition and cleavage property of IdeS makes this method applicable to a broad range of Fc fusion proteins having either standard or non-canonical hinge regions.

KEYWORDS:

Fc fusion protein; Glycosylation analysis; IdeS protease; LC-MS

PMID:
23839239
PMCID:
PMC3851216
DOI:
10.4161/mabs.25302
[Indexed for MEDLINE]
Free PMC Article
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