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Isolation of salivary MUC7 with gel electrophoresis allowed analysis by LC-MS and LC-MS(2) of released O-linked oligosaccharides and a thorough description of the glycosylation of this molecule, where high-molecular-weight oligosaccharides up to the size of 2790 Da and with up to three sialic acid residues were identified. A common theme of these novel high(More)
Goblet cells specialize in producing and secreting mucus with its main component, mucins. An inducible goblet-like cell line was used for the purification of the mucus vesicles stored in these cells by density gradient ultracentrifugation, and their proteome was analyzed by nanoLC-MS and MS/MS. Although the density of these vesicles coincides with others,(More)
This study aimed to characterize human salivary glycoforms and the natural glycosylation variation of the major ABO blood group bearing high molecular weight glycoprotein fraction MG1, which mainly consists of MUC5B mucin. Reduced and alkylated mucins from individuals of blood group A, B, and O were purified by sodium dodecyl sulfate-agarose/polyacrylamide(More)
We have analyzed the structures of the glycans on immunoprecipitated proteins from small amounts of cell or tissue lysates, by liquid-chromatography electrospray mass spectrometry (LC-ESI-MS) and MS/MS. The sensitive and specific method was applied to the analysis of the O-glycosylation of MUC1 in breast, prostate and gastric cancer, including analysis of a(More)
The polymeric mucin MUC2 constitutes the main structural component of the mucus that covers the colon epithelium. The protein's central mucin domain is highly O-glycosylated and binds water to provide lubrication and prevent dehydration, binds bacteria, and separates the bacteria from the epithelial cells. Glycosylation outside the mucin domain is suggested(More)
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