Oxidoreductase Activity of a Stable Multi-protein Complex from the Sea Cucumber Eupentacta fraudatrix.

Fuente: PubMed
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Autori principali: Tolmacheva, Anna S, Soboleva, Svetlana E, Ermakov, Evgeny A, Dmitrenok, Pavel S, Nevinsky, Georgy A
Natura: Artículo científico
Lingua:en
Pubblicazione: The protein journal 2026
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author Tolmacheva, Anna S
Soboleva, Svetlana E
Ermakov, Evgeny A
Dmitrenok, Pavel S
Nevinsky, Georgy A
author_facet Tolmacheva, Anna S
Soboleva, Svetlana E
Ermakov, Evgeny A
Dmitrenok, Pavel S
Nevinsky, Georgy A
Tolmacheva, Anna S
Soboleva, Svetlana E
Ermakov, Evgeny A
Dmitrenok, Pavel S
Nevinsky, Georgy A
collection PubMed - marine biology
contents Oxidoreductase Activity of a Stable Multi-protein Complex from the Sea Cucumber Eupentacta fraudatrix. Tolmacheva, Anna S Soboleva, Svetlana E Ermakov, Evgeny A Dmitrenok, Pavel S Nevinsky, Georgy A Bioactive compounds, such as peptides, proteins, and protein complexes, including those with antioxidant properties, are abundant in marine organisms. However, the antioxidant properties of protein complexes from sea cucumbers are underexplored. In this study, we show for the first time that a stable multi-protein complex (SMPC) from the sea cucumber E. fraudatrix possesses oxidoreductase activities. The SMPC was obtained by sequential gel-filtration on Sepharose 4B and Sephacryl S-1000 sorbent. Using a spectrophotometric method and an in situ activity assay, showed that the SMPC catalyzed hydrogen peroxide decomposition (specific activity 85.1 ± 4.4 mM H2O2/min/mg) as well as 3,3′-diaminobenzidine (DAB) and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) oxidation both in the presence (84.2 ± 3.1 mM/min/mg; 285.1 ± 11.2 mM/min/mg) or absence (61.4 ± 1.8 mM/min/mg; 178.3 ± 5.0 mM/min/mg) of hydrogen peroxide respectively. The data obtained showed that the SMPC from E. fraudatrix possesses oxidoreductase activities and can be involved in reactive oxygen species level regulation. This study highlighted the need for further research on SMPCs and their potential role in marine organisms.
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institution PubMed
language en
publishDate 2026
publisher The protein journal
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spellingShingle Oxidoreductase Activity of a Stable Multi-protein Complex from the Sea Cucumber Eupentacta fraudatrix.
Tolmacheva, Anna S
Soboleva, Svetlana E
Ermakov, Evgeny A
Dmitrenok, Pavel S
Nevinsky, Georgy A
Oxidoreductase Activity of a Stable Multi-protein Complex from the Sea Cucumber Eupentacta fraudatrix. Tolmacheva, Anna S Soboleva, Svetlana E Ermakov, Evgeny A Dmitrenok, Pavel S Nevinsky, Georgy A Bioactive compounds, such as peptides, proteins, and protein complexes, including those with antioxidant properties, are abundant in marine organisms. However, the antioxidant properties of protein complexes from sea cucumbers are underexplored. In this study, we show for the first time that a stable multi-protein complex (SMPC) from the sea cucumber E. fraudatrix possesses oxidoreductase activities. The SMPC was obtained by sequential gel-filtration on Sepharose 4B and Sephacryl S-1000 sorbent. Using a spectrophotometric method and an in situ activity assay, showed that the SMPC catalyzed hydrogen peroxide decomposition (specific activity 85.1 ± 4.4 mM H2O2/min/mg) as well as 3,3′-diaminobenzidine (DAB) and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) oxidation both in the presence (84.2 ± 3.1 mM/min/mg; 285.1 ± 11.2 mM/min/mg) or absence (61.4 ± 1.8 mM/min/mg; 178.3 ± 5.0 mM/min/mg) of hydrogen peroxide respectively. The data obtained showed that the SMPC from E. fraudatrix possesses oxidoreductase activities and can be involved in reactive oxygen species level regulation. This study highlighted the need for further research on SMPCs and their potential role in marine organisms.
title Oxidoreductase Activity of a Stable Multi-protein Complex from the Sea Cucumber Eupentacta fraudatrix.
url https://pubmed.ncbi.nlm.nih.gov/42050308/