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This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Mueller, S. Articles by Stremmel, W. Search for Related Content PubMed PubMed Citation Articles by Mueller, S. Articles by Stremmel, W. Related Collections Red Cells Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Direct Evidence for Catalase as the Predominant H2O2 -Removing Enzyme in Human Erythrocytes Sebastian Mueller, Hans-Dieter Riedel, and Wolfgang Stremmel From the Department of Internal Medicine IV, University of Heidelberg, Heidelberg, Germany. Decomposition of hydrogen peroxide (H2O2 ) at physiological levels was studied in human erythrocytes by means of a recently developed sensitive H2O2 assay. The exponential decay of H2O2 in the presence of purified erythrocyte catalase was followed down to 10-9 mol/L H2O2 at pH 7.4. H2O2 decomposition by purified erythrocyte glutathione peroxidase (GPO) could be directly observed down to 10-7 mol/L H2O2 . No enzyme inhibition was observed at these low H2O2 concentrations. Catalase and GPO activities can be determined separately in a titrated mixture of purified enzymes, which simulates the conditions of H2O2 removal by the erythrocyte. Experiments with fresh human hemolysate allowed us to determine H2O2 decomposition by catalase and GPO using these enzymes in their original quantitative ratio. The different kinetics of these enzymes are shown: H2O2 decomposition by catalase depends linearly on H2O2 concentration, whereas that by GPO becomes saturated at concentrations above 10-6 mol/L H2O2 . Even at very low H2O2 concentrations GPO reaches only approximately 8% of the rate at which catalase simultaneously degrades H2O2 . These data indicate an almost exclusive role for catalase in the removal of H2O2 in normal human erythrocytes. Blood, Vol. 90 No. 12 (December 15), 1997: pp. 4973-4978 © 1997 by The American Society of Hematology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Z. Lappalainen, J. Lappalainen, N. K. J. Oksala, D. E. Laaksonen, S. Khanna, C. K. Sen, and M. Atalay Diabetes impairs exercise training-associated thioredoxin response and glutathione status in rat brain J Appl Physiol, February 1, 2009; 106(2): 461 - 467. [Abstract] [Full Text] [PDF] A. S. Mueller, S. D. Klomann, N. M. Wolf, S. Schneider, R. Schmidt, J. Spielmann, G. Stangl, K. Eder, and J. Pallauf Redox Regulation of Protein Tyrosine Phosphatase 1B by Manipulation of Dietary Selenium Affects the Triglyceride Concentration in Rat Liver J. Nutr., December 1, 2008; 138(12): 2328 - 2336. [Abstract] [Full Text] [PDF] B. Andriopoulos, S. Hegedusch, J. Mangin, H.-D. Riedel, U. Hebling, J. Wang, K. Pantopoulos, and S. Mueller Sustained Hydrogen Peroxide Induces Iron Uptake by Transferrin Receptor-1 Independent of the Iron Regulatory Protein/Iron-responsive Element Network J. Biol. Chem., July 13, 2007; 282(28): 20301 - 20308. [Abstract] [Full Text] [PDF] L. Goth, Z. Toth, I. Tarnai, M. Berces, P. Torok, and W. N. Bigler Blood Catalase Activity in Gestational Diabetes Is Decreased but Not Associated with Pregnancy Complications Clin. Chem., December 1, 2005; 51(12): 2401 - 2404. [Full Text] [PDF] Y.-S. Ho, Y. Xiong, W. Ma, A. Spector, and D. S. Ho Mice Lacking Catalase Develop Normally but Show Differential Sensitivity to Oxidant Tissue Injury J. Biol. Chem., July 30, 2004; 279(31): 32804 - 32812. [Abstract] [Full Text] [PDF] A. Salvador and M. A. Savageau Quantitative evolutionary design of glucose 6-phosphate dehydrogenase expression in human erythrocytes PNAS, November 25, 2003; 100(24): 14463 - 14468. [Abstract] [Full Text] [PDF] M. Davidovits, A. Barak, R. Cleper, I. Krause, Z. Gamzo, and B. Eisenstein Methaemoglobinaemia and haemolysis associated with hydrogen peroxide in a paediatric haemodialysis centre: a warning note Nephrol. Dial. Transplant., November 1, 2003; 18(11): 2354 - 2358. [Abstract] [Full Text] [PDF] S. Mutze, U. Hebling, W. Stremmel, J. Wang, J. Arnhold, K. Pantopoulos, and S. Mueller Myeloperoxidase-derived Hypochlorous Acid Antagonizes the Oxidative Stress-mediated Activation of Iron Regulatory Protein 1 J. Biol. Chem., October 17, 2003; 278(42): 40542 - 40549. [Abstract] [Full Text] [PDF] L. Goth, A. Lenkey, and W. N. Bigler Blood Catalase Deficiency and Diabetes in Hungary Diabetes Care, October 1, 2001; 24(10): 1839 - 1840. [Full Text] [PDF] R. M. Johnson, G. Goyette Jr, Y. Ravindranath, and Y.-S. Ho Red cells from glutathione peroxidase-1-deficient mice have nearly normal defenses against exogenous peroxides Blood, September 1, 2000; 96(5): 1985 - 1988. [Abstract] [Full Text] [PDF] L. Goth, A. Gorzsas, and T. Kalmar A Simple PCR-Heteroduplex Screening Method for Detection of a Common Mutation of the Catalase Gene in Hungary Clin. Chem., August 1, 2000; 46(8): 1199 - 1200. [Full Text] [PDF] S. Mueller, K. Pantopoulos, C. A. Hubner, W. Stremmel, and M. W. Hentze IRP1 Activation by Extracellular Oxidative Stress in the Perfused Rat Liver J. Biol. Chem., June 15, 2001; 276(25): 23192 - 23196. [Abstract] [Full Text] [PDF]

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