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

The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.

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

Open access

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

DOI 10.1182/blood.v87.4.1595.bloodjournal8741595

Open this paper in CoChat — free account Open PDF

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1182/blood.v87.4.1595.bloodjournal8741595

Cites

24 of 24 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

[13] Catalase in vitro
Aebi, H. (1984) · Methods in Enzymology · doi:10.1016/s0076-6879(84)05016-3 · Cited by 25,696
[44] Glutathione peroxidase
Wendel, A. (1981) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(81)77046-0 · Cited by 3,032
Red Cell Metabolism: A Manual of Biochemical Methods.
(1971) · Annals of Internal Medicine · doi:10.7326/0003-4819-75-6-985_1 · Cited by 2,327
HEMOGLOBIN CATABOLISM
Mills, G. C. (1957) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)70608-x · Cited by 799
The removal of leukocytes and platelets from whole blood.
Beutler, E., West, C., & Blume, K. G. (1976) · PubMed · Cited by 731
Red cell metabolism. A. Defects not causing hemolytic disease. B. Environmental modification.
Beutler, E. (1972) · PubMed · Cited by 701
Glutathione Peroxidase: The Primary Agent for the Elimination of Hydrogen Peroxide in Erythrocytes*
Cohen, G., & Hochstein, P. (1963) · Biochemistry · doi:10.1021/bi00906a038 · Cited by 666
Catalase: a tetrameric enzyme with four tightly bound molecules of NADPH.
Kirkman, H., & Gaetani, G. F. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.14.4343 · Cited by 476
Self-citation
An Improved Coupled Test Procedure for Glutathione Peroxidase (EC 1.11.1.9.) in Blood
Günzler, W. A., Kremers, H., & Flohé, L. (1974) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.1974.12.10.444 · Cited by 369
Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes
Gaetani, G., Galiano, S., Canepa, L., Ferraris, A., & Kirkman, H. (1989) · Blood · doi:10.1182/blood.v73.1.334.334 · Cited by 298
Self-citation

Show all 21 references

Research works printed but not linked: 1

Aebi H, Suter H: Protective function of reduced glutathione (G-SH) against the effect of peroxidative substances and of irradia- tion in the red cell, in FlohC L, Benohr H, Sies H, Waller HD, Wendell A (eds): Glutathione. Stuttgart, Germany, Thieme, 1974, p 198

Sorted by citations

Items 101–200 of 296

Effects of rs769217 and rs1001179 polymorphisms of catalase gene on blood catalase, carbohydrate and lipid biomarkers in diabetes mellitus
Góth, L., Nagy, T., Kósa, Z., Fejes, Z., Bhattoa, H. P., Paragh, G., & Káplár, M. (2012) · Free Radical Research · doi:10.3109/10715762.2012.702899 · Cited by 35
Designing self-propelled, chemically active sheets: Wrappers, flappers, and creepers
Laskar, A., Shklyaev, O. E., & Balazs, A. C. (2018) · Science Advances · doi:10.1126/sciadv.aav1745 · Cited by 32
Oxidative stress in older patients with iron deficiency anaemia
Baccin, A. C., Lazzaretti, L. L., Brandao, V. D. M., Manfredini, V., Peralba, M. C. R., & Benfato, M. S. (2009) · The journal of nutrition health & aging · doi:10.1007/s12603-009-0195-6 · Cited by 34
Catalase-dependent H 2 O 2 consumption by cardiac mitochondria and redox-mediated loss in insulin signaling
Rindler, P. M., Cacciola, A., Kinter, M. T., & Szweda, L. I. (2016) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00066.2016 · Cited by 32
Glutathione Reverses Endothelial Damage From Peroxynitrite, the Byproduct of Nitric Oxide Degradation, in Crystalloid Cardioplegia
Nakamura, M., Thourani, V. H., Ronson, R. S., Velez, D. A., L, X., Katzmark, S. L., Robinson, J. A., Schmarkey, L. S., Zhao, Z., Wang, N., et al. (2000) · Circulation · doi:10.1161/01.cir.102.suppl_3.iii-332 · Cited by 32
Effects of Replacing Yellow Corn with Olive Cake Meal on Growth Performance, Plasma Lipid Profile, and Muscle Fatty Acid Content in Broilers
Saleh, A. A., & Alzawqari, M. H. (2021) · Animals · doi:10.3390/ani11082240 · Cited by 31
Decreased Activity of Erythrocyte Catalase and Glutathione Peroxidase in Patients with Schizophrenia
Djordjevic, V., Kostić, J., Krivokapić, Ž., Krtinić, D., Ranković, M., Petković, M., & Ćosić, V. (2022) · Medicina · doi:10.3390/medicina58101491 · Cited by 30
JAK2V617F mediates resistance to DNA damage-induced apoptosis by modulating FOXO3A localization and Bcl-xL deamidation
Ahn, J. S., Li, J., Chen, E., Kent, D. G., Park, H. J., & Green, A. R. (2015) · Oncogene · doi:10.1038/onc.2015.285 · Cited by 31
Exenatide improves hepatic steatosis by enhancing lipid use in adipose tissue in nondiabetic rats
Tanaka, K. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i10.2653 · Cited by 29
Synergistic effect of selenium and UV-B radiation in enhancing antioxidant level of wheatgrass grown from selenium rich wheat
Jaiswal, S. K., Prakash, R., Skalny, A. V., Геннадиевна, С. М., Grabeklis, A. R., Skalnaya, A. A., Tinkov, A. A., Zhang, F., Guo, X., & Prakash, N. T. (2018) · Journal of Food Biochemistry · doi:10.1111/jfbc.12577 · Cited by 28
Antioxidant effect of Zanthoxylum limonella Alston.
Tangjitjaroenkun, J. (2012) · Journal of Medicinal Plants Research · doi:10.5897/jmpr10.846 · Cited by 27
Melanin directly converts light for vertebrate metabolic use: Heuristic thoughts on birds, Icarus and dark human skin
Goodman, G., & Bercovich, D. (2008) · Medical Hypotheses · doi:10.1016/j.mehy.2008.03.038 · Cited by 27
Comparison of antioxidant activity of insulin, Ocimum gratissimum L., and Vernonia amygdalina L. in type 1 diabetic rat model
Okon, U. A., & Umoren, I. U. (2017) · Journal of Chinese Integrative Medicine · doi:10.1016/s2095-4964(17)60332-7 · Cited by 27
Catalase Enzyme Mutations and their Association with Diseases
G??th, L., Rass, P., & y, A. P. (2004) · Molecular Diagnosis · doi:10.2165/00066982-200408030-00001 · Cited by 27
In ovo injection of nano‐selenium spheres mitigates the hatchability, histopathology image and immune response of hatched chicks
El‐Deep, M. H., Amber, K. A., Elgendy, S. A., Dawood, M. A. O., & Zidan, A. (2020) · Journal of Animal Physiology and Animal Nutrition · doi:10.1111/jpn.13379 · Cited by 26
Catalase deficiency may complicate urate oxidase (rasburicase) therapy
Góth, L., & Bigler, N. W. (2007) · Free Radical Research · doi:10.1080/10715760701482451 · Cited by 25
Detection of a novel familial catalase mutation (Hungarian type D) and the possible risk of inherited catalase deficiency for diabetes mellitus
Góth, L., Vitai, M., Rass, P., Sükei, E., & Páy, A. (2005) · Electrophoresis · doi:10.1002/elps.200410384 · Cited by 25
Protective Effects of Molsidomine Against Cisplatin-Induced Nephrotoxicity
Karakoc, H. T. E., Altıntaş, R., Parlakpınar, H., Polat, A., Şamdancı, E., Sağır, M., & Duran, Z. R. (2015) · Advances in Clinical and Experimental Medicine · doi:10.17219/acem/58970 · Cited by 24
Role of c-miR-21, c-miR-126, Redox Status, and Inflammatory Conditions as Potential Predictors of Vascular Damage in T2DM Patients
López-Armas, G. D. C., Yessenbekova, A., González-Castañeda, R. E., Arellano-Arteaga, K. J., Guerra‐Librero, A., Аблайханова, Н. Т., Florido, J., Escames, G., Acuña-Castroviejo, D., & Rusanova, I. (2022) · Antioxidants · doi:10.3390/antiox11091675 · Cited by 23
Effects of Selenium Dietary Yeast on Growth Performance, Slaughter Performance, Antioxidant Capacity, and Selenium Deposition in Broiler Chickens
Liu, J., Wang, Z., Li, C., Chen, Z., Zheng, A., Chang, W., Liu, G., & Cai, H. (2023) · Animals · doi:10.3390/ani13243830 · Cited by 28
Changes of voltage-dependent anion-selective channel proteins VDAC1 and VDAC2 brain levels in patients with Alzheimer's disease and Down Syndrome
Yoo, B. C., Fountoulakis, M., Cairns, N. J., & Lübec, G. (2001) · Electrophoresis · doi:10.1002/1522-2683(200101)22:1 · Cited by 130
Effect of C111T polymorphism in exon 9 of the catalase gene on blood catalase activity in different types of diabetes mellitus
Tarnai, I., Csordás, M., Sükei, E., Shemirani, A. H., Káplár, M., & Góth, L. (2007) · Free Radical Research · doi:10.1080/10715760701381778 · Cited by 24
Flavonoids from Heliotropium subulatum exudate and their evaluation for antioxidant, antineoplastic and cytotoxic activities II
Singh, B., Sahu, P. M., & Sharma, R. A. (2016) · Cytotechnology · doi:10.1007/s10616-016-0041-8 · Cited by 24
In Vitro and in Vivo Antioxidant Effects and the Possible Relationship between the Antidepression Efficacy of Traditional Chinese Medicine Formulation Chaihu Shugan San
Li, S., Su, Z., Peng, J., Zou, Z., & Yu, C. (2010) · Chinese Journal of Natural Medicines · doi:10.1016/s1875-5364(10)60042-8 · Cited by 24
Oxidative stress, hemato-immunological, and intestinal morphometry changes induced by ochratoxin A in APRI rabbits and the protective role of probiotics
El‐Deep, M. H., Amber, K. A., Elgendy, S. A., Dawood, M. A. O., Elwakeel, E. M., & Paray, B. A. (2020) · Environmental Science and Pollution Research · doi:10.1007/s11356-020-09837-3 · Cited by 23
Intracellular redox equilibrium is essential for the constitutive expression of AP-1 dependent genes in resting cells: Studies on TGF-β1 regulation
González-Ramos, M., Mora, I., de Frutos, S., Garesse, R., Rodrı́guez-Puyol, M., Olmos, G., & Rodrı́guez-Puyol, D. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.03.003 · Cited by 23
Biophysical perspective of the binding of ester-functionalized gemini surfactants with catalase
Akram, M., Bhat, I. A., Anwar, S., Ahmad, A., & KABIR‐UD‐DIN, K. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.04.011 · Cited by 23
Potential Antioxidant Activity of New Tetracyclic and Pentacyclic Nonlinear Phenothiazine Derivatives
Engwa, G. A., Ayuk, E. L., Igbojekwe, B. U., & Unaegbu, M. (2016) · Biochemistry Research International · doi:10.1155/2016/9896575 · Cited by 23
Membrane Skeletal Protein S -Glutathionylation in Human Red Blood Cells as Index of Oxidative Stress
Giustarini, D., Dalle‐Donne, I., Milzani, A., Braconi, D., Santucci, A., & Rossi, R. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.8b00408 · Cited by 23
Effect of Light Wavelengths and Coherence on Growth, Enzymes Activity, and Melanin Accumulation of Liquid-Cultured Inonotus obliquus (Ach.:Pers.) Pilát
Poyedinok, N. L., Mykhaylova, O. B., Tugay, T. I., Tugay, A., Negriyko, A. M., & Dudka, I. O. (2015) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-015-1577-3 · Cited by 23
Study of oxidative stress in peripheral blood of Indian vitiligo patients
Deo, S., Bhagat, A., & Shah, R. (2013) · Indian Dermatology Online Journal · doi:10.4103/2229-5178.120637 · Cited by 23
Reduction of Carbon Tetrachloride-Induced Rat Liver Injury by Coffee and Green Tea
Noori, S., Rehman, N., Qureshi, M., & Mahboob, T. (2009) · Pakistan Journal of Nutrition · doi:10.3923/pjn.2009.452.458 · Cited by 23
Polymorphism of 5′ of the catalase gene in Hungarian acatalasemia and hypocatalasemia
Góth, L., & Vitai, M. (1997) · Electrophoresis · doi:10.1002/elps.1150180714 · Cited by 23
Cystathionine beta synthase deficiency induces catalase-mediated hydrogen peroxide detoxification in mice liver
Hamelet, J., Seltzer, V., Petit, E., Noll, C., Andréau, K., Delabar, J. M., & Janel, N. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.05.003 · Cited by 22
The effects of in ovo feeding of selenized glucose on liver selenium concentration and antioxidant capacity in neonatal broilers
Li, J., Shi, Q., Xue, Y., Zheng, M., Liu, L., Geng, T., Gong, D., & Zhao, M. (2023) · Chinese Chemical Letters · doi:10.1016/j.cclet.2023.109239 · Cited by 22
Immune and anti-oxidant effects of in ovo selenium proteinate on post-hatch experimental avian necrotic enteritis
Lee, S. H., Lillehoj, H. S., Jang, S. I., Jeong, M., Kim, D., Xu, S., Lee, S. K., Kim, J. B., Park, H. J., Kim, H.-R., et al. (2014) · Veterinary Parasitology · doi:10.1016/j.vetpar.2014.10.025 · Cited by 22
Catalase activity and arsenic sensitivity in acute leukemia
Coe, E., & Schimmer, A. D. (2008) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428190802353617 · Cited by 22
Vanillin and Vanillin Analogs Relax Porcine Coronary and Basilar Arteries by Inhibiting L-Type Ca2+ Channels
Raffai, G., Khang, G., & Vanhoutte, P. M. (2014) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.217935 · Cited by 22
Electrochemical Red Blood Cell Counting: One at a Time
Sepunaru, L., Sokolov, S. V., Holter, J., Young, N. P., & Compton, R. G. (2016) · Angewandte Chemie · doi:10.1002/ange.201605310 · Cited by 22
The Promising Role of Microbiome Therapy on Biomarkers of Inflammation and Oxidative Stress in Type 2 Diabetes: A Systematic and Narrative Review
Paul, P., Kaul, R., Abdellatif, B., Arabi, M., Upadhyay, R., Saliba, R., Sebah, M., & Châari, A. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.906243 · Cited by 22
Anemia Caused by Oxidative Stress
Iuchi, Y. (2012) · InTech eBooks · doi:10.5772/31404 · Cited by 22
Aspergillus awamori positively impacts the growth performance, nutrient digestibility, antioxidative activity and immune responses of growing rabbits
El‐Deep, M. H., Dawood, M. A. O., Assar, M. H., & Paray, B. A. (2020) · Veterinary Medicine and Science · doi:10.1002/vms3.345 · Cited by 21
Lymphaticovenous Anastomosis Supermicrosurgery Decreases Oxidative Stress and Increases Antioxidant Capacity in the Serum of Lymphedema Patients
Yang, J. C., Huang, L., Wu, S., Kuo, P., Wu, Y.-C., Wu, C., Lin, C.-W., Tsai, P.-Y., & Hsieh, C. (2021) · Journal of Clinical Medicine · doi:10.3390/jcm10071540 · Cited by 21
Improved catalytic activity by catalase immobilization using γ‐cyclodextrin and electrospun PCL nanofibers
Canbolat, M. F., Savaş, H. B., & Gültekin, F. (2016) · Journal of Applied Polymer Science · doi:10.1002/app.44404 · Cited by 21
Oxidative stress adaptation improves the heat tolerance of Pseudomonas fluorescens SN15-2
Chen, J., Wang, X., Tang, D., & Wang, W. (2019) · Biological Control · doi:10.1016/j.biocontrol.2019.104070 · Cited by 19
Dietary Replacement Effect of Fish Meal by Tuna By-Product Meal on Growth and Feed Availability of Red Sea Bream (Pagrus major)
Baek, S. I., & Cho, S. H. (2024) · Animals · doi:10.3390/ani14050688 · Cited by 20
Influence of green tea on erythrocytes antioxidant status of different age rats intoxicated with ethanol
Łuczaj, W., Zapora, E., & Skrzydlewska, E. (2009) · Phytotherapy Research · doi:10.1002/ptr.2986 · Cited by 20
Substituting fishmeal with extruded soybean meal in diets did not affect the growth performance, hepatic enzyme activities, but hypoxia tolerance of Dolly Varden (Salvelinus malma) juveniles
Meng, F., Li, B., Xie, Y., Li, M., & Wang, R. (2019) · Aquaculture Research · doi:10.1111/are.14385 · Cited by 20
Effect of Selenium on Performance, Egg Quality, Egg Selenium Content and Serum Antioxidant Capacity in Laying Hens
Hu, L., Yu, Q., Tang, X., Fang, C., Chen, S., & Fang, R. (2020) · Pakistan Journal of Zoology · doi:10.17582/journal.pjz/20190424040448 · Cited by 20
Chemically controlled shape-morphing of elastic sheets
Manna, R. K., Shklyaev, O. E., Stone, H. A., & Balazs, A. C. (2020) · Materials Horizons · doi:10.1039/d0mh00730g · Cited by 20
VOLATILE CONSTITUENTS AND ANTIOXIDANT PROPERTY OF ESSENTIAL OIL FROM PLECTRANTHUS AMBOINICUS (LOUR)
Grace, V. M. B. (2012) · International Journal of Pharma and Bio Sciences · Cited by 19
Evaluation of Biological Indicators of Fatigue and Muscle Damage in Arabian Horses After Race
Mami, S., Gh.H., K., Shahriari, A., & Gooraninejad, S. (2019) · Journal of Equine Veterinary Science · doi:10.1016/j.jevs.2019.04.007 · Cited by 19
β‐Carotene, α‐tocopherol and ascorbic acid: differential profile of antioxidant, inflammatory status and regulation of gene expression in human mononuclear cells of diabetic donors
de Oliveira, B. F., Costa, D. C., Nogueira‐Machado, J. A., & Chaves, M. M. (2013) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.2439 · Cited by 20
Biomarkers of Oxidative Stress and Their Clinical Relevance in Type 2 Diabetes Mellitus Patients: A Systematic Review
Sabitha, S., Hegde, S. V., Agarwal, S. V., Delna, N. S., Pillai, A., Shah, S. N., & Ramjeela, S. (2024) · Cureus · doi:10.7759/cureus.66570 · Cited by 31
Genetic heterogeneity of the 5′ uncoding region of the catalase gene in Hungarian acatalasemic and hypocatalasemic subjects
Góth, L. (1998) · Clinica Chimica Acta · doi:10.1016/s0009-8981(97)00243-x · Cited by 18
Contributions of spinal d-amino acid oxidase to chronic morphine-induced hyperalgesia
Ma, S., Li, X., Gong, N., & Wang, Y. (2015) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2015.03.021 · Cited by 18
Catalase and chondroitin sulfate derivatives against thrombotic effect induced by reactive oxygen species in a rat artery
Maksimenko, A. V., Golubykh, V. L., & Tischenko, E. G. (2003) · Metabolic Engineering · doi:10.1016/s1096-7176(03)00026-0 · Cited by 18
ANTIOXIDANT PROPERTIES OF SINAPIC ACID: IN VITRO AND IN VIVO APPROACH
Nithya, R., & Subramanian, S. P. (2017) · Asian Journal of Pharmaceutical and Clinical Research · doi:10.22159/ajpcr.2017.v10i6.18263 · Cited by 19
Comparative effect of horse gram and black gram on inflammatory mediators and antioxidant status
Rajagopal, V., Pushpan, C. K., & Helen, A. (2016) · Journal of Food and Drug Analysis · doi:10.1016/j.jfda.2016.08.010 · Cited by 18
Vernonia amygdalina (Del) as an antioxidant, aspirin toxicity, and oxidative stress
Alabi, Q. K., & Adeyemi, W. J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819092-0.00048-0 · Cited by 18
The Effect of Ginger (Zingiber officinale) on Oxidative Stress Status in the Small Intestine of Diabetic Rats
Taghavi, M. M., & Sedigheh, F. S. (2008) · Cited by 17
Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose‐6‐phosphate dehydrogenase‐deficient erythrocytes from newborn infants
Cheah, F., Peskin, A. V., Wong, F., Ithnin, A., Othman, A., & Winterbourn, C. C. (2014) · The FASEB Journal · doi:10.1096/fj.14-250050 · Cited by 17
Glutathione Reverses Endothelial Damage From Peroxynitrite, the Byproduct of Nitric Oxide Degradation, in Crystalloid Cardioplegia
Nakamura, M., Thourani, V. H., Ronson, R. S., Velez, D. A., Ma, X., Katzmark, S. L., Robinson, J. A., Schmarkey, L. S., Zhao, Z., Wang, N.-P., et al. (2000) · Circulation · doi:10.1161/circ.102.suppl_3.iii-332 · Cited by 17
Effect of cyprodinil and fludioxonil pesticides on bovine liver catalase activity
Karadağ, H., & Ozhan, F. (2015) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2014.992740 · Cited by 16
Electrochemistry of catalase at a liquid|liquid micro-interface array
Zannah, S., & Arrigan, D. W. M. (2020) · Bioelectrochemistry · doi:10.1016/j.bioelechem.2020.107694 · Cited by 15
Biochemical composition and activities of digestive and antioxidant enzymes during the egg and yolk‐sac larval development of the cobia ( Rachycentron canadum )
Huang, J., Amenyogbe, E., Chen, G., & Wang, W. (2020) · Aquaculture Research · doi:10.1111/are.15017 · Cited by 15
On human health
Spijk, P. V. (2014) · Medicine Health Care and Philosophy · doi:10.1007/s11019-014-9602-9 · Cited by 16
Inhibitory Effects of ECQ on Indomethacin-Induced Gastric Damage in Rats
Jung, J.-H., Nam, Y., & Sohn, U. D. (2012) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2012.16.6.399 · Cited by 15
Oxytocin ameliorates cisplatin-induced nephrotoxicity in Wistar rats
Elberry, A. A., Refaie, S. M., Kamel, M. W., Ali, T. M., Darwish, H., & Ashour, O. M. (2013) · Annals of Saudi Medicine · doi:10.5144/0256-4947.2013.57 · Cited by 15
Collaboration and competition between active sheets for self-propelled particles
Laskar, A., Shklyaev, O. E., & Balazs, A. C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1901235116 · Cited by 15
Function of the endophytic fungus Acrophialophora jodhpurensis, methionine, and nitric oxide in wheat resistance induction against Fusarium graminearum via interplay of reactive oxygen species and iron
Daroodi, Z., & Taheri, P. (2023) · Physiological and Molecular Plant Pathology · doi:10.1016/j.pmpp.2023.102132 · Cited by 14
Enzymatic cascade reactors on carbon nanotube transistor detecting trace prostate cancer biomarker
Liu, W., Wang, X., Dong, B., Liu, Y., & Wei, D. (2024) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2024.116603 · Cited by 14
Avaliação de parâmetros antioxidantes em ratos tratados com sevoflurano
Bezerra, F. J. L., do Vale, N. B., Macedo, B. D. O., de Rezende, A. A., & Almeida, M. D. G. (2010) · Brazilian Journal of Anesthesiology · doi:10.1016/s0034-7094(10)70021-0 · Cited by 14
Effects of Selenium on Tebuconazole-Induced Hepatotoxicity in Adult Rats
Saad, H. B., Kammoun, I., Boudawara, T. S., Km, Z., Hakim, A., & Amara, I. (2017) · Research and reviews in biosciences · Cited by 14
Hypolipidemic and Antioxidative Effects of African Star Apple Juice (Chrysophylum albidum) on Rats Fed on Diets High in Cholesterol and Oil
Bobadoye, M. F., Bamisi, O. O., & Enujiugha, V. N. (2016) · Food and Nutrition Sciences · doi:10.4236/fns.2016.710083 · Cited by 15
Sub-Chronic Toxicity of the Hydroethanolic Leaf Extract of Telfairia occidentalis Hook. f. (Cucurbitaceae) in Male Rats
Akindele, A. J., Oladimeji-Salami, J. A., Oyetola, R. A., & Osiagwu, D. D. (2018) · Medicines · doi:10.3390/medicines5010004 · Cited by 14
Interplay between Erythrocyte Peroxidases and Membrane
Melo, D., Rocha, S., Coimbra, S., & Santos‐Silva, A. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.83590 · Cited by 14
Cerium Oxide-Based Nanozymes in Biology and Medicine
Yadav, N., Patel, V., & Singh, S. (2019) · Springer proceedings in physics · doi:10.1007/978-981-15-0202-6_15 · Cited by 14
Over expression of glutamate cysteine ligase increases cellular resistance to H2O2‐induced DNA single‐strand breaks
Shi, S., Hudson, F. N., Botta, D., McGrath, M. B., White, C. C., Neff‐LaFord, H. D., Dabrowski, M. J., Singh, N. P., & Kavanagh, T. J. (2007) · Cytometry Part A · doi:10.1002/cyto.a.20434 · Cited by 14
Evaluation of the salivary level of glutathione reductase, catalase and free thiol in patients with oral lichen planus
Rezazadeh, F., Mahdavi, D., Fassihi, N., Sedarat, H., Khorami, E. T., & Tabesh, A. (2023) · BMC Oral Health · doi:10.1186/s12903-023-03242-1 · Cited by 13
Sodium Selenium Enhances the Antioxidative Activities and Immune Functions of Apis mellifera (Hymenoptera: Apidae) and Increases the Selenium Content in Royal Jelly
Chi, X., Wei, W., Zhang, W., Liu, Z., Wang, H., & Xu, B. (2019) · Environmental Entomology · doi:10.1093/ee/nvz131 · Cited by 13
Mitochondrial unfolded protein response in regulatory T cell function: a protective mechanism in immune aging
Lewis, L., Valvi, D., Gedaly, R., & Martí, F. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1621759 · Cited by 12
Myocardial Infarction
Singh, A., & Jat, R. K. (2022) · Himalayan Journal of Health Sciences · doi:10.22270/hjhs.v6i4.116 · Cited by 12
ANTIDIABETIC AND ENZYMATIC ANTIOXIDANT POTENTIAL FROM ETHANOLIC EXTRACTS OF LEAF AND FRUIT OF TRICHOSANTHES DIOICA AND LEAF OF CLITORIA TERNATEA ON DIABETIC RATS INDUCED BY STREPTOZOTOCIN
Kavitha, R. (2018) · Asian Journal of Pharmaceutical and Clinical Research · doi:10.22159/ajpcr.2018.v11i5.24434 · Cited by 12
Nociceptin Increases Antioxidant Expression in the Kidney, Liver and Brain of Diabetic Rats
Adeghate, E. A., D’Souza, C. M., Saeed, Z., Jaberi, S. A., Tariq, S., Kalász, H., Tekes, K., & Adeghate, E. A. (2021) · Biology · doi:10.3390/biology10070621 · Cited by 12
The influence of the duration of the expulsive stage of parturition on the occurrence of postpartum oxidative stress in sows with uncomplicated, spontaneous farrowings
Szczubiał, M., Dąbrowski, R., Bochniarz, M., & Komar, M. (2013) · Theriogenology · doi:10.1016/j.theriogenology.2013.05.015 · Cited by 11
Potential adverse effects of oseltamivir in rats: males are more vulnerable than females
El-Sayed, W. M., & Al‐Kahtani, M. A. (2011) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y11-060 · Cited by 11
A Laboratory Study on the Modeling of Temperature-Dependent Development and Antioxidant System of Chilo suppressalis (Lepidoptera: Crambidae)
Shamakhi, L., Zibaee, A., Karimi‐Malati, A., & Hoda, H. (2018) · Journal of Insect Science · doi:10.1093/jisesa/iey027 · Cited by 11
Functional and structural analysis of double and triple mutants reveals the contribution of protein instability to clinical manifestations of G6PD variants
Praoparotai, A., Junkree, T., Imwong, M., & Boonyuen, U. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.05.026 · Cited by 11
Controlling the Spatiotemporal Transport of Particles in Fluid-Filled Microchambers
Laskar, A., Shklyaev, O. E., & Balazs, A. C. (2020) · Langmuir · doi:10.1021/acs.langmuir.9b03546 · Cited by 10
Antioxidative system in the erythrocytes of preterm neonates with sepsis: the effects of vitamin E supplementation
Bajčetić, M., Otašević, B., Božinović-Prekajski, N., Spasić, S. D., & Spasojević, I. (2013) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1177/0004563213503317 · Cited by 10
Simple PCR heteroduplex, SSCP mutation screening methods for the detection of novel catalase mutations in Hungarian patients with type 2 diabetes mellitus
Vitai, M., Fátrai, S., Rass, P., Csordás, M., & Tarnai, I. (2005) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2005.230 · Cited by 10
ANTIOXIDANT ACTIVITY OF RHIZOME EXTRACTS OF COLEUS FORSKOHLII BRIQ
Shanmugam, S., Rani, U., V, & Pradeep, B. V. (2018) · Asian Journal of Pharmaceutical and Clinical Research · doi:10.22159/ajpcr.2018.v11i11.27125 · Cited by 10
The genus Acrophialophora: History, phylogeny, morphology, beneficial effects and pathogenicity
Daroodi, Z., & Taheri, P. (2024) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2024.103875 · Cited by 9
Catalase Inhibition by Aminoalkanol Derivatives with Potential Anti-Cancer Activity—In Vitro and In Silico Studies Using Capillary Electrophoresis Method
Grodner, B., Napiórkowska, M., & Pisklak, D. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137123 · Cited by 9
Using a Hands-On Hydrogen Peroxide Decomposition Activity To Teach Catalysis Concepts to K–12 Students
Cybulskis, V. J., Ribeiro, F. H., & Gounder, R. (2016) · Journal of Chemical Education · doi:10.1021/acs.jchemed.5b00946 · Cited by 9
Multivitamin solutions for enteral supplementation
Laborie, S., Lavoie, J., Rouleau, T., & Chessex, P. (2002) · Nutrition · doi:10.1016/s0899-9007(02)00742-6 · Cited by 9
Dietary lipid concentrations influence growth, body composition, morphology of the liver and mid-intestine, and antioxidant status of marbled eel (Anguilla marmorata)
Chen, S., Liu, P., Jia, Y., Liao, H., Zhu, S.-X., Zhou, L., Dan, X., Liu, L., Li, J., Zheng, S.-B., et al. (2020) · Aquaculture International · doi:10.1007/s10499-020-00590-5 · Cited by 9
l-carnitine as a Potential Additive in Blood Storage Solutions: A Study on Erythrocytes
Soumya, R., Carl, H., & Rajashekaraiah, V. (2015) · Indian Journal of Hematology and Blood Transfusion · doi:10.1007/s12288-015-0569-3 · Cited by 9
Protective effect of D-ribose against inhibition of rats testes function at excessive exercise
Chigrinski, E. A., & Conway, V. (2011) · DOAJ (DOAJ: Directory of Open Access Journals) · Cited by 9

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

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks