Identification of novel glycosylation events on human serum-derived factor IX.
Beam-type collision-induced dissociation
Coagulation factors
Electron-transfer dissociation
Glycoproteomics
N-linked glycosylation
O-linked glycosylation
Journal
Glycoconjugate journal
ISSN: 1573-4986
Titre abrégé: Glycoconj J
Pays: United States
ID NLM: 8603310
Informations de publication
Date de publication:
08 2020
08 2020
Historique:
received:
28
11
2019
accepted:
24
03
2020
revised:
06
03
2020
pubmed:
8
5
2020
medline:
10
6
2021
entrez:
8
5
2020
Statut:
ppublish
Résumé
Human Factor IX is a highly post-translationally modified protein that is an important clotting factor in the blood coagulation cascade. Functional deficiencies in Factor IX result in the bleeding disorder haemophilia B, which is treated with plasma-derived or recombinant Factor IX concentrates. Here, we investigated the post-translational modifications of human serum-derived Factor IX and report previously undescribed O-linked monosaccharide compositions at serine 141 and a novel site of glycosylation. At serine 141 we observed two monosaccharide compositions, with HexNAc
Identifiants
pubmed: 32378017
doi: 10.1007/s10719-020-09922-2
pii: 10.1007/s10719-020-09922-2
doi:
Substances chimiques
Monosaccharides
0
Serine
452VLY9402
Factor IX
9001-28-9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM