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Abstract
Deciphering the pattern and abundance of O-glycosylation of mucin domain proteins, glycoproteins heavily implicated in cancer and other diseases, remains an ongoing challenge. Both the macro- and micro-heterogeneity of glycosylation complicates the analysis, motivating the development of new strategies for structural characterization of this diverse class of glycoproteins. Here we combine digestion of mucin domain proteins using a targeted protease, Enhancin from Serratia marcescens (SmE), with ultraviolet photodissociation (UVPD) mass spectrometry to advance glycan mapping and elucidation of O-glycosylation trends of densely glycosylated mucin proteins. UVPD facilitates identification of O-glycoforms of mucin domain proteins TIM-1, MUC-1 and MUC-16. Additionally, UVPD elucidates several glycoforms of MUC-16 and unravels O-glycosylation across tandem repeats of MUC-1.
Supplementary materials
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Supporting Tables
Description
Tables of identified fragments from various spectra within the document. A table detailing the glycoforms of MUC-16 at identified glycosites.
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Title
Supporting Figures
Description
File containing all supporting figures which includes spectra, pie graphs, Euler plots, sequence maps, and chromatograms.
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