N-glycans of bovine submaxillary mucin contain core-fucosylated and sulfated glycans but not sialylated glycans.
Bovine submaxillary mucin
Glycosylation site
N-glycan analysis
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Oct 2019
01 Oct 2019
Historique:
received:
09
04
2019
revised:
21
06
2019
accepted:
17
07
2019
pubmed:
22
7
2019
medline:
28
1
2020
entrez:
21
7
2019
Statut:
ppublish
Résumé
Bovine submaxillary mucin (BSM) is a heavily-glycosylated macromolecular (approximately 4 MDa) protein and is used in various biomaterial applications in light of its high viscosity and biocompatibility, in addition to use as a biochemical substrate or inhibitor as a result of its abundant O-glycans. Although it has been reported that N-glycosylation provides stability of human mucins, most BSM research has been focused on its O-glycans, while N-glycans have not been reported to date. In this study, a common N-glycan core component was detected by monosaccharide analysis of BSM, and the structures of the N-glycans and their relative quantities were determined by liquid chromatography-tandem mass spectrometry. Seventeen N-glycans comprising ten complex-type [Fucose
Identifiants
pubmed: 31325506
pii: S0141-8130(19)32496-1
doi: 10.1016/j.ijbiomac.2019.07.108
pii:
doi:
Substances chimiques
Monosaccharides
0
Mucins
0
Polysaccharides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1072-1078Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.