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Hydrophilic interaction chromatography coupled to ultraviolet photodissociation affords identification, localization, and relative quantitation of glycans on intact glycoproteins

ABSTRACT: Protein glycosylation is implicated in a wide array of diseases, yet glycoprotein analysis remains elusive owing to the extreme heterogeneity of glycans including microheterogeneity at the same amino acid residue (glycosite). Top-down mass spectrometry (MS) allows precise identification and localization of glycans on intact proteins, and coupling top-down MS with chromatography allows time-resolved characterization of glycoforms. Here, we couple ultraviolet photo-dissociation (UVPD) to hydrophilic interaction chromatography (HILIC) to advance the characterization of glycoproteins ranging from 15-34 kDa, offering site localization of glycans, providing sequence coverages up to 93% and relative quan-titation of individual glycoforms.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Jennifer Brodbelt

PROVIDER: PXD050098 | JPOST Repository | Sat Feb 24 00:00:00 GMT 2024

REPOSITORIES: jPOST

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			Action	DRS
	20230815_VKJ_nano1_HILICmonolithTFA_RNaseB.raw	Raw
	20230825_VKJ_nano1_HILICmonolithTFA_RNAseB1.raw	Raw
	20230925_VKJ_nano1_HILICmonolithTFA_RNaseB_UVPD_50avg1pls2mJ2.raw	Raw
	20230925_VKJ_nano1_HILICmonolithTFA_RNaseB_std.raw	Raw
	20230928_VKJ_nano1_HILICmonolithTFA_RBD_o-gly.raw	Raw

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