Cited by 296Redox biology and oxidative stressAntioxidant Activity and Oxidative StressGlutathione Transferases and Polymorphisms

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Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes

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Gaetani, GF, Ferraris, AM, Rolfo, M, Mangerini, R, Arena, S, Kirkman, HN·1996·Blood

DOI 10.1182/blood.v87.4.1595.bloodjournal8741595

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Abstract

Purified enzymes were mixed to form a cell-free system that simulated the conditions for removal of hydrogen peroxide within human erythrocytes. Human glutathione peroxidase disposed of hydrogen peroxide (H2O2) at a rate that was only 17% of the rate at which human catalase simultaneously removed hydrogen peroxide. The relative rates observed were in agreement with the relative rates predicted from the kinetic constants of the two enzymes. These results confirm two earlier studies on intact erythrocytes, which refuted the notion that glutathione peroxidase is the primary enzyme for removal of hydrogen peroxide within erythrocytes. The present findings differ from the results with intact cells, however, in showing that glutathione peroxidase accounts for even less than 50% of the removal of hydrogen peroxide. A means is proposed for calculating the relative contribution of glutathione peroxidase and catalase in other cells and species. The present results raise the possibility that the major function of glutathione peroxidase may be the disposal of organic peroxides rather than the removal of hydrogen peroxide.

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Authors: Gaetani, G., Ferraris, A., Rolfo, M., Mangerini, R., Arena, S., & Kirkman, H.
Affiliations: University of Genoa (IT)
Division of Hematological Oncology, Istituto Nazionale per la Ricerca sul Cancro, University of Genoa, Italy.
Venue: Blood
Publisher: American Society of Hematology
Published: 1996-02-15
Volume: 87
Issue: 4
Pages: 1595-1599
ISSN: 0006-4971 (ISSN-L)
1528-0020
DOI: 10.1182/blood.v87.4.1595.bloodjournal8741595
OpenAlex: W160949418
Cited by: 296
References: 21
Citations by year: 2026: 2 · 2025: 3 · 2024: 12 · 2023: 12 · 2022: 13 · 2021: 11 · 2020: 15 · 2019: 23 · 2018: 14 · 2017: 13 · 2016: 15 · 2015: 17 · 2014: 25 · 2013: 15 · 2012: 17
FWCI: 1.64
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Blood (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Biochemistry (medical) › Antioxidant Activity and Oxidative Stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords: catalase, glutathione peroxidase, hydrogen peroxide, erythrocytes, cell-free system, enzyme kinetics, antioxidant enzymes
MeSH terms: Catalase, Cell-Free System, Erythrocytes, Gluconates, Glutathione, Glutathione Peroxidase, Humans, Hydrogen Peroxide, NAD

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Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes

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