Glutathione Peroxidase: The Primary Agent for the Elimination of Hydrogen Peroxide in Erythrocytes*
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTGlutathione Peroxidase: The Primary Agent for the Elimination of Hydrogen Peroxide in Erythrocytes*Gerald Cohen and Paul HochsteinCite this: Biochemistry 1963, 2, 6, 1420–1428Publication Date (Print):November 1, 1963Publication History Published online1 May 2002Published inissue 1 November 1963https://pubs.acs.org/doi/10.1021/bi00906a038https://doi.org/10.1021/bi00906a038research-articleACS PublicationsRequest reuse permissionsArticle Views928Altmetric-Citations530LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In nonpathological conditions, glutathione peroxidase is the enzyme degrading most of the H2O2 by oxidizing reduced GSH into GSSG.
“In nonpathological conditions, GPx has been shown to be the enzyme degrading most of the H2O2 by oxidizing reduced GSH into GSSG (Eq. 10).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [38]
Cites
The Metabolic Basis of Inherited Disease.
(1988) · Annals of Internal Medicine · doi:10.7326/0003-4819-108-3-503_7 · Cited by 7,807 · see citing works
MICRODETERMINATION OF OXYHEMOGLOBIN, METHEMOGLOBIN, AND SULFHEMOGLOBIN IN A SINGLE SAMPLE OF BLOOD
Evelyn, K. A., & Malloy, H. T. (1938) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)73873-8 · Cited by 1,189 · see citing works
Mills, G. C. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70608-x · Cited by 799 · see citing works
Beutler, E. (1957) · PubMed · Cited by 457 · see citing works
Properties of catalase. Catalysis of coupled oxidation of alcohols
Keilin, D., & Hartree, E. F. (1945) · Biochemical Journal · doi:10.1042/bj0390293 · Cited by 440 · see citing works
A modification of the nitroprusside method of analysis for glutathione.
Rr, G., & PHILLIPS, P. H. (1951) · PubMed · Cited by 333 · see citing works
Tarlov, A. R. (1962) · Archives of Internal Medicine · doi:10.1001/archinte.1962.03620140081013 · Cited by 275 · see citing works
The Purification and Properties of Glutathione Peroxidase of Erythrocytes
Mills, G. C. (1959) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70234-2 · Cited by 241 · see citing works
Catalase, peroxidase and metmyoglobin as catalysts of coupled peroxidatic reactions
Keilin, D., & Hartree, E. F. (1955) · Biochemical Journal · doi:10.1042/bj0600310 · Cited by 176 · see citing works
Glutathione peroxidase and the destruction of hydrogen peroxide in animal tissues
Mills, G. C. (1960) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(60)90357-x · Cited by 146 · see citing works
Glucose-6-Phosphate Dehydrogenase and Detoxification of Hydrogen Peroxide in Human Erythrocytes
Cohen, G., & Hochstein, P. E. (1961) · Science · doi:10.1126/science.134.3492.1756 · Cited by 114 · see citing works
Self-citationWoodward, G. E. (1935) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)75210-1 · Cited by 88 · see citing works
ON THE REACTION OF CATALASE PEROXIDES WITH ACCEPTORS
Chance, B. (1950) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)56500-5 · Cited by 88 · see citing works
The reduction of oxidized glutathione in erythrocyte haemolysates in pernicious anaemia
Jocelyn, P. C. (1960) · Biochemical Journal · doi:10.1042/bj0770363 · Cited by 37 · see citing works
KAZIRO, K., Kikuchi, G., Nakamura, H., et al. (1952) · Chemische Berichte · doi:10.1002/cber.19520850909 · Cited by 15 · see citing works
Biosynthesis of glutathione in human blood cells.
KOJ, A. (1962) · PubMed · Cited by 12 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Lubos, E., Loscalzo, J., & Handy, D. E. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3586 · Cited by 1,280 · see citing works
Radical-free biology of oxidative stress
Jones, D. P. (2008) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00283.2008 · Cited by 1,213 · see citing works
Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism
Wong, G. H. W., & Goeddel, D. V. (1988) · Science · doi:10.1126/science.3263703 · Cited by 914 · see citing works
Metabolic Regulation of Hematopoietic Stem Cells in the Hypoxic Niche
Suda, T., Takubo, K., & Semenza, G. L. (2011) · Cell Stem Cell · doi:10.1016/j.stem.2011.09.010 · Cited by 844 · see citing works
Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
Kuhn, V., Diederich, L., Keller, T. C. S., Kramer, C. M., Lückstädt, W., Panknin, C., Suvorava, T., Isakson, B. E., Kelm, M., & Cortese-Krott, M. M. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6954 · Cited by 469 · see citing works
Fisher, A. B. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3412 · Cited by 410 · see citing works
Lipid peroxidation in erythrocytes
Clemens, M. R., & Waller, H. D. (1987) · Chemistry and Physics of Lipids · doi:10.1016/0009-3084(87)90068-5 · Cited by 318 · see citing works
Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes
Gaetani, G., Ferraris, A., Rolfo, M., Mangerini, R., Arena, S., & Kirkman, H. (1996) · Blood · doi:10.1182/blood.v87.4.1595.bloodjournal8741595 · Cited by 296 · see citing works
Gaetani, G., Galiano, S., Canepa, L., Ferraris, A., & Kirkman, H. (1989) · Blood · doi:10.1182/blood.v73.1.334.334 · Cited by 298 · see citing works
Hemoglobin autoxidation and regulation of endogenous H2O2 levels in erythrocytes
Johnson, R. M., Goyette, G., Ravindranath, Y., & Ho, Y.-S. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.07.002 · Cited by 185 · see citing works
Inborn defects in the antioxidant systems of human red blood cells
van Zwieten, R., Verhoeven, A. J., & Roos, D. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.11.022 · Cited by 179 · see citing works
Rybka, J., Kędziora-Kornatowska, K., Banaś-Leżańska, P., Majsterek, I., Carvalho, L. A., Cattaneo, A., Anacker, C., & Kędziora, J. (2013) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.05.019 · Cited by 146 · see citing works
Reactive Species in Sickle Cell Disease
ASLAN, M., THORNLEY‐BROWN, D., & FREEMAN, B. A. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06201.x · Cited by 136 · see citing works
Role of free radicals in the pathogenesis of acute chest syndrome in sickle cell disease
Klings, E. S., & Farber, H. W. (2001) · Respiratory Research · doi:10.1186/rr70 · Cited by 132 · see citing works
Brownlee, N. R., Huttner, J. J., Panganamala, R. V., & Cornwell, D. G. (1977) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41605-0 · Cited by 99 · see citing works
The kinetic mechanism of glutathione peroxidase from human platelets
Ramos Martínez, J. I., Díaz García, R., & Galarza, A. M. (1982) · Thrombosis Research · doi:10.1016/0049-3848(82)90199-2 · Cited by 11 · see citing works
- Authors
- Cohen, G., & Hochstein, P.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1963-11-01
- Volume
- 2
- Issue
- 6
- Pages
- 1420-1428
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2053985315
- Cited by
- 666
- References
- 16
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 9 · 2023: 8 · 2022: 6 · 2021: 6 · 2020: 4 · 2019: 6 · 2018: 6 · 2017: 6 · 2016: 10 · 2015: 14 · 2014: 13 · 2013: 9 · 2012: 8
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- glutathione peroxidase, hydrogen peroxide, erythrocytes, antioxidant enzymes, erythrocyte metabolism
- MeSH terms
- Animals, Biological Transport, Catalase, Erythrocytes, Glutathione, Glutathione Peroxidase, Hemolysis, Hydrogen Peroxide, Metabolism, Methemoglobin, Peroxidases, Poultry, Research, Cell Death
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review