Top-Down ETD-MS Provides Unreliable Quantitation of Methionine Oxidation.
Apoproteins
/ analysis
Calmodulin
/ analysis
Hydrogen Peroxide
/ chemistry
Hydroxyl Radical
/ chemistry
Methionine
/ analysis
Myoglobin
/ analysis
Oxidation-Reduction
Peptides
/ analysis
Protein Footprinting
Protein Processing, Post-Translational
Proteins
/ analysis
Reproducibility of Results
Tandem Mass Spectrometry
/ methods
hydroxyl radical protein footprinting
post-translational modification
proteomics
Journal
Journal of biomolecular techniques : JBT
ISSN: 1943-4731
Titre abrégé: J Biomol Tech
Pays: United States
ID NLM: 100888641
Informations de publication
Date de publication:
12 2019
12 2019
Historique:
pubmed:
31
10
2019
medline:
16
5
2020
entrez:
31
10
2019
Statut:
ppublish
Résumé
Methionine oxidation plays a critical role in many processes of biologic and biomedical importance, including cellular redox responses and stability of protein pharmaceuticals. Bottom-up methods for analysis of methionine oxidation can suffer from incomplete sequence coverage, as well as an inability to readily detect correlated oxidation between 2 or more methionines. However, the methodology for quantifying protein oxidation in top-down analyses is lacking. Previous work has shown that electron transfer dissociation (ETD)-based tandem mass spectrometry (MS/MS) fragmentation offers accurate and precise quantification of amino acid oxidation in peptides, even in complex samples. However, the ability of ETD-based MS/MS fragmentation to accurately quantify amino acid oxidation of proteins in a top-down manner has not been reported. Using apomyoglobin and calmodulin as model proteins, we partially converted methionines into methionine sulfoxide by incubation in H
Identifiants
pubmed: 31662705
doi: 10.7171/jbt.19-3004-002
pii: JBT_2019-3004-002
pmc: PMC6808186
doi:
Substances chimiques
Apoproteins
0
Calmodulin
0
Myoglobin
0
Peptides
0
Proteins
0
apomyoglobin
0
Hydroxyl Radical
3352-57-6
Methionine
AE28F7PNPL
Hydrogen Peroxide
BBX060AN9V
Types de publication
Journal Article
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
50-57Informations de copyright
© Association of Biomolecular Resource Facilities.
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