Structural and quantitative characterization of mucin-type O-glycans and the identification of Oglycosylation sites in bovine submaxillary mucin
DC Field | Value | Language |
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dc.contributor.author | Kim J. | - |
dc.contributor.author | Ryu C. | - |
dc.contributor.author | Ha J. | - |
dc.contributor.author | Lee J. | - |
dc.contributor.author | Kim D. | - |
dc.contributor.author | Ji M. | - |
dc.contributor.author | Park C.S. | - |
dc.contributor.author | Lee J. | - |
dc.contributor.author | Kim D.K. | - |
dc.contributor.author | Kim H.H. | - |
dc.date.available | 2020-08-03T06:27:04Z | - |
dc.date.issued | 2020-04 | - |
dc.identifier.issn | 2218-273X | - |
dc.identifier.issn | 2218-273X | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/42748 | - |
dc.description.abstract | 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 1μg of BSM) were identified with 14 major (>1.0%), 12 minor (0.1%-1.0%), and eight trace (<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;56SGETRTSVI,259SHSSSGRSRTI,272GSPSSVSSAEQI,307RPSYGAL,625QTLGPL,728TMTTRTSVVV, and1080RPEDNTAVA) 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. © 2020 by the authors. Licensee MDPI, Basel, Switzerland. | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | MDPI AG | - |
dc.title | Structural and quantitative characterization of mucin-type O-glycans and the identification of Oglycosylation sites in bovine submaxillary mucin | - |
dc.type | Article | - |
dc.identifier.doi | 10.3390/biom10040636 | - |
dc.identifier.bibliographicCitation | Biomolecules, v.10, no.4 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000539492400140 | - |
dc.identifier.scopusid | 2-s2.0-85083964730 | - |
dc.citation.number | 4 | - |
dc.citation.title | Biomolecules | - |
dc.citation.volume | 10 | - |
dc.type.docType | Article | - |
dc.publisher.location | 스위스 | - |
dc.subject.keywordAuthor | Bovine submaxillary mucin | - |
dc.subject.keywordAuthor | Mucin-type O-glycan | - |
dc.subject.keywordAuthor | O-glycosylation site | - |
dc.subject.keywordPlus | glycan | - |
dc.subject.keywordPlus | glycopeptide | - |
dc.subject.keywordPlus | glycosyltransferase | - |
dc.subject.keywordPlus | microcrystalline cellulose | - |
dc.subject.keywordPlus | mucin | - |
dc.subject.keywordPlus | affinity chromatography | - |
dc.subject.keywordPlus | amino acid sequence | - |
dc.subject.keywordPlus | anion exchange chromatography | - |
dc.subject.keywordPlus | Article | - |
dc.subject.keywordPlus | controlled study | - |
dc.subject.keywordPlus | flow rate | - |
dc.subject.keywordPlus | glycosylation | - |
dc.subject.keywordPlus | high performance liquid chromatography | - |
dc.subject.keywordPlus | ion exchange chromatography | - |
dc.subject.keywordPlus | mass fragmentography | - |
dc.subject.keywordPlus | nonhuman | - |
dc.subject.keywordPlus | polyacrylamide gel electrophoresis | - |
dc.subject.keywordPlus | polymerization | - |
dc.subject.keywordPlus | protein analysis | - |
dc.subject.keywordPlus | protein determination | - |
dc.subject.keywordPlus | protein purification | - |
dc.subject.keywordPlus | protein structure | - |
dc.subject.keywordPlus | retention time | - |
dc.subject.keywordPlus | sensitivity and specificity | - |
dc.subject.keywordPlus | sialylation | - |
dc.subject.keywordPlus | ultra performance liquid chromatography | - |
dc.subject.keywordPlus | viscoelasticity | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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