Reversible Oxidative Modifications in Myoglobin and Functional Implications.

ditryptophan dityrosine myoglobin peroxidase protein aggregation

Journal

Antioxidants (Basel, Switzerland)
ISSN: 2076-3921
Titre abrégé: Antioxidants (Basel)
Pays: Switzerland
ID NLM: 101668981

Informations de publication

Date de publication:
24 Jun 2020
Historique:
received: 28 04 2020
revised: 14 06 2020
accepted: 18 06 2020
entrez: 1 7 2020
pubmed: 1 7 2020
medline: 1 7 2020
Statut: epublish

Résumé

Myoglobin (Mb), an oxygen-binding heme protein highly expressed in heart and skeletal muscle, has been shown to undergo oxidative modifications on both an inter- and intramolecular level when exposed to hydrogen peroxide (H

Identifiants

pubmed: 32599765
pii: antiox9060549
doi: 10.3390/antiox9060549
pmc: PMC7346209
pii:
doi:

Types de publication

Journal Article

Langues

eng

Subventions

Organisme : NIDDK NIH HHS
ID : R15 DK102122
Pays : United States
Organisme : NIDDK NIH HHS
ID : R15DK102122
Pays : United States

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Auteurs

Mark H Mannino (MH)

Department of Biology, Saint Louis University, St. Louis, MO 63103, USA.

Rishi S Patel (RS)

Department of Biology, Saint Louis University, St. Louis, MO 63103, USA.

Amanda M Eccardt (AM)

Department of Biology, Saint Louis University, St. Louis, MO 63103, USA.

Blythe E Janowiak (BE)

Department of Biology, Saint Louis University, St. Louis, MO 63103, USA.

David C Wood (DC)

Department of Biochemistry and Molecular Biology, Saint Louis University, St. Louis, MO 63104, USA.

Fahu He (F)

Department of Chemistry, Saint Louis University, St. Louis, MO 63103, USA.

Jonathan S Fisher (JS)

Department of Biology, Saint Louis University, St. Louis, MO 63103, USA.

Classifications MeSH