Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes.
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Summary
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.
- Type
- article
- Published
- 1996-02-15
- Cited by
- 308
- References
- 22
- Access
- Open access
- OpenAlex
- https://openalex.org/W160949418
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:1769780
Keywords
Hydrogen peroxide, Catalase, Peroxidase, Chemistry, Glutathione peroxidase
References
- Erythrocyte defense against hydrogen peroxide: preeminent importance of catalase.
- The removal of leukocytes and platelets from whole blood.
- Catalase in vitro.
- NADPH, not glutathione, status modulates oxidant sensitivity in normal and glucose-6-phosphate dehydrogenase-deficient erythrocytes.
- Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes.
- Regulation of glucose-6-phosphate dehydrogenase in human erythrocytes.
- The function of catalase-bound NADPH.
- Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown.
- Decreased catalase activity is the underlying mechanism of oxidant susceptibility in glucose-6-phosphate dehydrogenase-deficient erythrocytes.
- Erythrocyte catalase. A somatic oxidant defense?
- Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH.
- GLUTATHIONE PEROXIDASE: THE PRIMARY AGENT FOR THE ELIMINATION OF HYDROGEN PEROXIDE IN ERYTHROCYTES.
- OXIDATIVE HEMOLYSIS AND ERYTHROCYTE METABOLISM IN HEREDITARY ACATALASIA.
- An Improved Coupled Test Procedure for Glutathione Peroxidase (EC 1.11.1.9.) in Blood
- Catalase activity and red cell metabolism.
- Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes.
- Red cell metabolism
- [Glutathione peroxidase].
- Red Cell Metabolism: A Manual of Biochemical Methods.
- Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes
Cited by
- Silibinin induced autophagic and apoptotic cell death in HT1080 cells through a reactive oxygen species pathway.
- Catalase-dependent H2O2 consumption by cardiac mitochondria and redox-mediated loss in insulin signaling.
- Influence of antioxidant genotype and antioxidant status on progression of chronic kidney disease
- Protective effect of D-ribose against inhibition of rats testes function at excessive exercise
- In vitro reconstitution of the entire enterocin biosynthetic pathway: New insights into type II PKS enzymology
- Catalase attenuates pulmonary fibrosis while increasing pro-inflammatory cytokines
- Serum xanthine oxidase profile in stressed Marwari sheep from arid tracts in India
- Analyse du rôle de la NADPH oxydase et du stress oxydant dans les cellules dendritiques
- Effect of air, peroxides and diabetes on antioxidant enzyme localization in red blood cells
- Affinity enrichment and mass spectrometric quantitation of protein carbonyls
- The impact of oxidative stress and potential antioxidant therapy on function and survival of cultured pancreatic β-islet cells
- l-carnitine as a Potential Additive in Blood Storage Solutions: A Study on Erythrocytes
- Serum biomarkers of physiological defense against reactive oxygen species during environmental stress in Indian dromedaries.
- Studies on effect of stabilizers, chelators and inherent periodicity on nanoparticle antioxidant activity
- Oxidants and antioxidants of erythrocytes
- JAK2V617F mediates resistance to DNA damage-induced apoptosis by modulating FOXO3A localization and Bcl-xL deamidation
- Redox State Of Erythrocyte Peroxiredoxin 2 During Oxidative Stress And Its Effect On Membrane Binding
- Blood antioxidant parameters in sickle cell anemia patients in steady state.
- Erythrocyte: Bacteria Killer and Bacteria Pray
- Antioxidant Activities, Nutrient Composition and Sensory Properties of Unripe Plantain-Purple Skinned Sweet Potato Flour Blends
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