PMC:7108637 / 14007-15090 JSONTXT

{"project":"2_test","denotations":[{"id":"29579213-21542793-45167291","span":{"begin":310,"end":314},"obj":"21542793"},{"id":"29579213-25660649-45167292","span":{"begin":331,"end":335},"obj":"25660649"},{"id":"29579213-25452148-45167293","span":{"begin":350,"end":354},"obj":"25452148"},{"id":"29579213-14674469-45167294","span":{"begin":710,"end":714},"obj":"14674469"},{"id":"29579213-26208004-45167295","span":{"begin":727,"end":731},"obj":"26208004"},{"id":"29579213-14674469-45167296","span":{"begin":939,"end":943},"obj":"14674469"},{"id":"29579213-20131323-45167297","span":{"begin":960,"end":964},"obj":"20131323"},{"id":"T33111","span":{"begin":310,"end":314},"obj":"21542793"},{"id":"T53760","span":{"begin":331,"end":335},"obj":"25660649"},{"id":"T52927","span":{"begin":350,"end":354},"obj":"25452148"},{"id":"T80416","span":{"begin":710,"end":714},"obj":"14674469"},{"id":"T27742","span":{"begin":727,"end":731},"obj":"26208004"},{"id":"T61855","span":{"begin":939,"end":943},"obj":"14674469"},{"id":"T98534","span":{"begin":960,"end":964},"obj":"20131323"}],"text":"Modern mass spectrometry-based methods of analysis enable robust characterization of N- or O-linked glycans in complex biological samples with unprecedented sensitivity and resolution. It has become routine practice in the characterization of recombinant therapeutics as well as vaccine candidates (Xie et al. 2011; Dubayle et al. 2015; Jacob et al. 2015). Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is one of the most commonly used tools in modern day glycan analysis. Combining MALDI-MS with lectin microarray enables more reliable characterization of glycan structures, where lectin binding profiles can provide additional information on the glycosidic linkage (Mechref et al. 2003; Lei et al. 2015). Moreover, tandem MALDI-MS or tandem electrospray ionization MS allows fragmentation of selected precursor ions, enabling more detailed characterization of structures of a given composition (Mechref et al. 2003; Ritchie et al. 2010). The techniques were soon adapted for analysis of N-glycans on recombinant viral proteins and mature viral particles."}