Catalyst-free Click PEGylation reveals substantial mitochondrial ATP synthase sub-unit alpha oxidation before and after fertilisation.
Adenosine Triphosphate
/ biosynthesis
Amino Acid Sequence
Animals
Click Chemistry
/ methods
Disulfides
/ chemistry
Embryo, Nonmammalian
Female
Fertilization in Vitro
Glutathione
/ metabolism
Heterocyclic Compounds, 1-Ring
/ chemistry
Male
Mitochondria
/ chemistry
Mitochondrial Proton-Translocating ATPases
/ chemistry
Ovum
/ chemistry
Oxidation-Reduction
Phylogeny
Polyethylene Glycols
/ chemistry
Protein Processing, Post-Translational
Protein Subunits
/ chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Sulfhydryl Compounds
/ chemistry
Xenopus laevis
/ classification
ATP synthase
Development
Fertilisation
Mitochondria
Redox signalling
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
09 2019
09 2019
Historique:
received:
20
05
2019
revised:
10
06
2019
accepted:
15
06
2019
pubmed:
25
6
2019
medline:
29
2
2020
entrez:
25
6
2019
Statut:
ppublish
Résumé
Using non-reducing Western blotting to assess protein thiol redox state is challenging because most reduced and oxidised forms migrate at the same molecular weight and are, therefore, indistinguishable. While copper catalysed Click chemistry can be used to ligate a polyethylene glycol (PEG) moiety termed Click PEGylation to mass shift the reduced or oxidised form as desired, the potential for copper catalysed auto-oxidation is problematic. Here we define a catalyst-free trans-cyclooctene-methyltetrazine (TCO-Tz) inverse electron demand Diels Alder chemistry approach that affords rapid (k ~2000 M
Identifiants
pubmed: 31234016
pii: S2213-2317(19)30563-4
doi: 10.1016/j.redox.2019.101258
pmc: PMC6597785
pii:
doi:
Substances chimiques
Disulfides
0
Heterocyclic Compounds, 1-Ring
0
Protein Subunits
0
Sulfhydryl Compounds
0
Polyethylene Glycols
3WJQ0SDW1A
Adenosine Triphosphate
8L70Q75FXE
Mitochondrial Proton-Translocating ATPases
EC 3.6.3.-
Glutathione
GAN16C9B8O
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
101258Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 212942/Z/18/Z
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R014841/1
Pays : United Kingdom
Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier B.V. All rights reserved.
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