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Bovine submaxillary mucin (BSM) is a gel-forming glycoprotein polymer, and Ser/Thr-linked glycans ( O -glycans) are important in regulating BSM's viscoelasticity and polymerization. However, details of O -glycosylation have not been reported. This study investigates the structural and quantitative characteristics of O -glycans and identifies O -glycosylation sites in BSM using liquid chromatography-tandem mass spectrometry. The O -glycans (consisting of di- to octa-saccharides) and their quantities (%) relative to total O -glycans (100%; 1.1 pmol per 1 μg of BSM) were identified with 14 major (&gt;1.0%), 12 minor (0.1%-1.0%), and eight trace (&lt;0.1%) O -glycans, which were characterized based on their constituents (sialylation (14 O -glycans; 81.9%, sum of relative quantities of each glycan), non-sialylation (20; 18.1%), fucosylation (20; 17.5%), and terminal-galactosylation (6; 3.6%)) and six core structure types [Gal-GalNAc, Gal-(GlcNAc)GalNAc, GlcNAc-GalNAc, GlcNAc-(GlcNAc)GalNAc, and GalNAc-GalNAc]. O -glycosylation sites were identified using O -glycopeptides (bold underlined; 56  S GE T R TS VI, 259  S H SSS GR S R T I, 272 G S P SS V SS AEQI, 307 RP S YGAL, 625 Q T LGPL, 728  T M TT R TS VVV, and 1080 RPEDN T AVA) obtained from proteolytic BSM; these sites are in the four domains of BSM. The gel-forming mucins share common domain structures and glycosylation patterns; these results could provide useful information on mucin-type O -glycans. This is the first study to characterize O -glycans and identify O -glycosylation sites in BSM.

Structural and Quantitative Characterization of Mucin-Type O-Glycans and the Identification of O-Glycosylation Sites in Bovine Submaxillary Mucin