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Article

Asymmetric N-Glycosylation in the Tailpiece of Recombinant IgA1

6 Dec 2024

Abstract excerpt

High Resolution Image Download MS PowerPoint Slide Here, we employed a variety of mass spectrometry (MS)-based approaches, both (glyco)peptide-centric and protein-centric, to resolve the complex glycoproteoform landscape of recombinant IgA1 produced in HEK293 cells. These key immunoglobulins harbor several N - and O -glycosylation sites, making them considerably more heterogeneous than their IgG counterparts. We...

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PMID: 39641195
DOI: 10.1021/jacs.4c13156

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