Characterization of N-glycosylations in Entamoeba histolytica ubiquitin.
Electrophoresis, Polyacrylamide Gel
Entamoeba histolytica
/ chemistry
Gas Chromatography-Mass Spectrometry
Glycosylation
Mass Spectrometry
/ methods
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
/ metabolism
Periodic Acid-Schiff Reaction
Polysaccharides
/ chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Trophozoites
/ chemistry
Ubiquitin
/ genetics
Continuous elution electrophoresis
Entamoeba histolytica
GC-MS
MALDI-TOF MS
N-Glycans
NSI-MS/MS
Ubiquitin
Journal
Experimental parasitology
ISSN: 1090-2449
Titre abrégé: Exp Parasitol
Pays: United States
ID NLM: 0370713
Informations de publication
Date de publication:
Jan 2019
Jan 2019
Historique:
received:
14
04
2018
revised:
10
11
2018
accepted:
13
11
2018
pubmed:
18
11
2018
medline:
16
1
2019
entrez:
17
11
2018
Statut:
ppublish
Résumé
Entamoeba histolytica harbors an extensive intracellular distribution of ubiquitin-proteasome systems important for numerous cellular processes. However, glycosylation studies of ubiquitin-proteasome components have not yet been elucidated. Here we report the partial characterization of N-linked glycosylation profile in E. histolytica ubiquitin by Fluorophore-Assisted Carbohydrate Electrophoresis (FACE), Nanoelectrospray Ionization-Tandem Mass Spectrometry (NSI-MS), Matrix-Assisted Laser-Desorption time-of-flight Mass Spectrometry (MALDI-TOF MS) and Gas Chromatography-Mass Spectrometry (GC-MS) analysis. To our knowledge, the data presented in this report represents the first structural glycomics analysis of E. histolytica ubiquitin, while most of the reports are performed on whole parasitic glycan profiles. The glycan profile of E. histolytica ubiquitin has high mannose N-glycan structures. The N-linked glycan profile showed fragments from Hex
Identifiants
pubmed: 30444974
pii: S0014-4894(18)30193-0
doi: 10.1016/j.exppara.2018.11.003
pii:
doi:
Substances chimiques
Polysaccharides
0
Ubiquitin
0
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
EC 3.5.1.52
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
38-47Informations de copyright
Copyright © 2018 Elsevier Inc. All rights reserved.