Peroxide-Induced Damage to Plasminogen Molecules.
antioxidant methionines
electrophoresis
hydrogen peroxide
mass spectrometry
oxidation
oxidation sites
plasminogen/plasmin
Journal
Doklady. Biochemistry and biophysics
ISSN: 1608-3091
Titre abrégé: Dokl Biochem Biophys
Pays: United States
ID NLM: 101126895
Informations de publication
Date de publication:
Nov 2021
Nov 2021
Historique:
received:
19
05
2021
accepted:
17
07
2021
revised:
16
07
2021
entrez:
30
12
2021
pubmed:
31
12
2021
medline:
12
2
2022
Statut:
ppublish
Résumé
Plasminogen is a zymogenic form of plasmin, an enzyme that plays a fundamental role in the dissolution of fibrin clots as well as in many other physiological processes. For the first time, by the method of gas chromatography-mass spectrometry, post-translational modifications in the primary structure of plasminogen treated with physiologically relevant amounts of hydrogen peroxide were identified. It was found that methionine and tryptophan residues located in different structural regions of plasminogen served as targets of the oxidant. Plasminogen oxidation caused a dose-dependent effect in decreasing the fibrinogenolytic activity of plasmin evidenced by the formation of fibrinogen degradation products. The possible antioxidant role of methionines in the oxidative modification of plasminogen is discussed.
Identifiants
pubmed: 34966964
doi: 10.1134/S1607672921060053
pii: 10.1134/S1607672921060053
doi:
Substances chimiques
Oxidants
0
Peroxides
0
Fibrin
9001-31-4
Fibrinogen
9001-32-5
Plasminogen
9001-91-6
Fibrinolysin
EC 3.4.21.7
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
419-423Informations de copyright
© 2021. Pleiades Publishing, Ltd.
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