Relevant bibliographies by topics / I> Peroxidase

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'I> Peroxidase'

Author: Grafiati
Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "I> Peroxidase"

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Missall, Tricia A., Jocie F. Cherry-Harris, and Jennifer K. Lodge. "Two glutathione peroxidases in the fungal pathogen Cryptococcus neoformans are expressed in the presence of specific substrates." Microbiology 151, no. 8 (2005): 2573–81. http://dx.doi.org/10.1099/mic.0.28132-0.

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Glutathione peroxidases catalyse the reduction of peroxides by reduced glutathione. To determine if these enzymes are important for resistance to oxidative stress and evasion of the innate immune system by the fungal pathogen Cryptococcus neoformans, two glutathione peroxidase homologues, which share 38 % identity, were identified and investigated. In this study, these peroxidases, Gpx1 and Gpx2, their localization, their contribution to total glutathione peroxidase activity, and their importance to the oxidative and nitrosative stress resistance of C. neoformans are described. It is shown tha
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Brenot, Audrey, Katherine Y. King, Blythe Janowiak, Owen Griffith, and Michael G. Caparon. "Contribution of Glutathione Peroxidase to the Virulence of Streptococcus pyogenes." Infection and Immunity 72, no. 1 (2004): 408–13. http://dx.doi.org/10.1128/iai.72.1.408-413.2004.

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ABSTRACT Glutathione peroxidases are widespread among eukaryotic organisms and function as a major defense against hydrogen peroxide and organic peroxides. However, glutathione peroxidases are not well studied among prokaryotic organisms and have not previously been shown to promote bacterial virulence. Recently, a gene with homology to glutathione peroxidase was shown to contribute to the antioxidant defenses of Streptococcus pyogenes (group A streptococcus). Since this bacterium causes numerous suppurative diseases that require it to thrive in highly inflamed tissue, it was of interest to de
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SAVITSKY, Pavel A., Irina G. GAZARYAN, Vladimir I. TISHKOV, L. Mark LAGRIMINI, Tautgirdas RUZGAS, and Lo GORTON. "Oxidation of indole-3-acetic acid by dioxygen catalysed by plant peroxidases: specificity for the enzyme structure." Biochemical Journal 340, no. 3 (1999): 579–83. http://dx.doi.org/10.1042/bj3400579.

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Indole-3-acetic acid (IAA) can be oxidized via two mechanisms: a conventional hydrogen-peroxide-dependent pathway, and one that is hydrogen-peroxide-independent and requires oxygen. It has been shown here for the first time that only plant peroxidases are able to catalyse the reaction of IAA oxidation with molecular oxygen. Cytochrome c peroxidase (CcP), fungal peroxidases (manganese-dependent peroxidase, lignin peroxidase and Arthromyces ramosus peroxidase) and microperoxidase were essentially inactive towards IAA in the absence of added H2O2. An analysis of amino acid sequences allowed five
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Vlasova, Irina. "Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control." Molecules 23, no. 10 (2018): 2561. http://dx.doi.org/10.3390/molecules23102561.

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The heme in the active center of peroxidases reacts with hydrogen peroxide to form highly reactive intermediates, which then oxidize simple substances called peroxidase substrates. Human peroxidases can be divided into two groups: (1) True peroxidases are enzymes whose main function is to generate free radicals in the peroxidase cycle and (pseudo)hypohalous acids in the halogenation cycle. The major true peroxidases are myeloperoxidase, eosinophil peroxidase and lactoperoxidase. (2) Pseudo-peroxidases perform various important functions in the body, but under the influence of external conditio
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Colon, Selene, Haiyan Luan, Yan Liu, Cameron Meyer, Leslie Gewin, and Gautam Bhave. "Peroxidasin and eosinophil peroxidase, but not myeloperoxidase, contribute to renal fibrosis in the murine unilateral ureteral obstruction model." American Journal of Physiology-Renal Physiology 316, no. 2 (2019): F360—F371. http://dx.doi.org/10.1152/ajprenal.00291.2018.

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Renal fibrosis is the pathological hallmark of chronic kidney disease (CKD) and manifests as glomerulosclerosis and tubulointerstitial fibrosis. Reactive oxygen species contribute significantly to renal inflammation and fibrosis, but most research has focused on superoxide and hydrogen peroxide (H2O2). The animal heme peroxidases myeloperoxidase (MPO), eosinophil peroxidase (EPX), and peroxidasin (PXDN) uniquely metabolize H2O2 into highly reactive and destructive hypohalous acids, such as hypobromous and hypochlorous acid. However, the role of these peroxidases and their downstream hypohalous
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Iturbe-Ormaetxe, Iñaki, Manuel A. Matamoros, Maria C. Rubio, David A. Dalton, and Manuel Becana. "The Antioxidants of Legume Nodule Mitochondria." Molecular Plant-Microbe Interactions® 14, no. 10 (2001): 1189–96. http://dx.doi.org/10.1094/mpmi.2001.14.10.1189.

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The mitochondria of legume root nodules are critical to sustain the energy-intensive process of nitrogen fixation. They also generate reactive oxygen species at high rates and thus require the protection of antioxidant enzymes and metabolites. We show here that highly purified mitochondria from bean nodules (Phaseolus vulgaris L. cv. Contender × Rhizobium leguminosarum bv. phaseoli strain 3622) contain ascorbate peroxidase primarily in the inner membrane (with lesser amounts detected occasionally in the matrix), guaiacol peroxidases in the outer membrane and matrix, and manganese superoxide di
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Gaetani, GF, AM Ferraris, M. Rolfo, R. Mangerini, S. Arena, and HN Kirkman. "Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes." Blood 87, no. 4 (1996): 1595–99. http://dx.doi.org/10.1182/blood.v87.4.1595.bloodjournal8741595.

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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
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Yadav, R. S. S., K. S. Yadav, and H. S. Yadav. "Luffa aegyptiaca (Gourd) Fruit Juice as a Source of Peroxidase." Enzyme Research 2011 (July 24, 2011): 1–5. http://dx.doi.org/10.4061/2011/319105.

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Peroxidases have turned out to be potential biocatalyst for a variety of organic reactions. The research work reported in this communication was done with the objective of finding a convenient rich source of peroxidase which could be used as a biocatalyst for organic synthetic reactions. The studies made have shown that Luffa aegyptiaca (gourd) fruit juice contains peroxidase activity of the order of 180 enzyme unit/mL. The Km values of this peroxidase for the substrates guaiacol and hydrogen peroxide were 2.0 and 0.2 mM, respectively. The pH and temperature optima were 6.5 and 60°C, respectiv
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Regelsberger, G., C. Jakopitsch, P. G. Furtmüller, et al. "The role of distal tryptophan in the bifunctional activity of catalase-peroxidases." Biochemical Society Transactions 29, no. 2 (2001): 99–105. http://dx.doi.org/10.1042/bst0290099.

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Catalase-peroxidases are bifunctional peroxidases exhibiting an overwhelming catalase activity and a substantial peroxidase activity. Here we present a kinetic study of the formation and reduction of the key intermediate compound I by probing the role of the conserved tryptophan at the distal haem cavity site. Two wild-type proteins and three mutants of Synechocystis catalase-peroxidase (W122A and W122F) and Escherichia coli catalase-peroxidase (W105F) have been investigated by steady-state and stopped-flow spectroscopy. W122F and W122A completely lost their catalase activity whereas in W105F
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Veal, Elizabeth A., Lewis E. Tomalin, Brian A. Morgan, and Alison M. Day. "The fission yeast Schizosaccharomyces pombe as a model to understand how peroxiredoxins influence cell responses to hydrogen peroxide." Biochemical Society Transactions 42, no. 4 (2014): 909–16. http://dx.doi.org/10.1042/bst20140059.

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As a more selectively reactive oxygen species, H2O2 (hydrogen peroxide) has been co-opted as a signalling molecule, but high levels can still lead to lethal amounts of cell damage. 2-Cys Prxs (peroxiredoxins) are ubiquitous thioredoxin peroxidases which utilize reversibly oxidized catalytic cysteine residues to reduce peroxides. As such, Prxs potentially make an important contribution to the repertoire of cell defences against oxidative damage. Although the abundance of eukaryotic 2-Cys Prxs suggests an important role in maintaining cell redox, the surprising sensitivity of their thioredoxin p
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Dissertations / Theses on the topic "I> Peroxidase"

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Lazzarotto, Fernanda. "Caracterização de um novo membro da superfamília de peroxidases não animais : ascorbato peroxidase-relacionada." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2015. http://hdl.handle.net/10183/131943.

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Peroxidases atuam catalisando a redução do peróxido de hidrogênio à água a fim de minimizar o dano celular e modular, direta ou indiretamente, respostas celulares dependentes da sinalização operada por esta espécie reativa de oxigênio. Análises prévias, feitas em bancos de dados de sequências genômicas, permitiram a identificação de uma nova heme peroxidase não-animal (ascorbato peroxidase-relacionada ou APx-R), a qual foi descrita pela primeira vez em 2011 em um estudo publicado pelo nosso grupo de pesquisa. O trabalho detalhado nos próximos capítulos desta tese teve como objetivo caracteriza
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Djerdjouri, Nour-Eddine. "Hydrogen peroxide delignification in a biomimetic system based on manganese peroxidase." Diss., Available online, Georgia Institute of Technology, 2005, 2003. http://etd.gatech.edu/theses/available/ipstetd-1017/.

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Loew, Noya. "Meerrettich Peroxidase : Modifikationen und Anwendungen in Biosensoren." Phd thesis, Universität Potsdam, 2008. http://opus.kobv.de/ubp/volltexte/2008/1843/.

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Biosensoren werden oft für die Messung einzelner Substanzen in komplexen Medien verwendet, wie z.B. bei der Blutzuckerbestimmung. Sie bestehen aus einem physikochemischen Sensor, dem Transduktionselement, und einer darauf immobilisierten biologischen Komponente, dem Erkennungselement. In dieser Arbeit wurde als Transduktionselement eine Elektrode und als Biokomponente das Enzym „Meerrettich Peroxidase“ (engl. horseradish peroxidase, HRP) verwendet. Solche HRP-Elektroden werden für die Messung von Wasserstoffperoxid (H2O2) eingesetzt. H2O2 wird im Körper von weißen Blutkörperchen produziert, um
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Houssain, Feroza. "Inhibitors of lignin peroxidase." Thesis, Imperial College London, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.283289.

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Adams, Ruqaiyah. "Characterization of a novel soybean candidate glutathione peroxidase/thioredoxin-dependent peroxidase under salt stress." Thesis, University of the Western Cape, 2012. http://hdl.handle.net/11394/3800.

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The study aimed to investigate the following: 1. Investigate a putative glutathione peroxidase gene (Glyma17g34110) within Glycine max by an in silico analysis and spatial expression. 2. Determine the effects of exogenously applied nitric oxide on the expression of Glyma17g34110. 3. Investigate the antioxidant mechanism with attention to Glyma17g34110,reactive oxygen species and cell death in the response to salt stress. 4. Establish whether Glyma17g34110 is a glutathione peroxidase or thioredoxindependent peroxidase gene.<br>Magister Scientiae - MSc
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Bartonek-Roxå, Eva. "Recombinant peroxidases and xylanases I. Cloning and production of a peroxidase from horseradish : II. Characterisation of functional domains of thermostable xylanases from Rhodothermus marinus /." Lund : Lund University, 1998. http://catalog.hathitrust.org/api/volumes/oclc/68945038.html.

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Phillips, Kyle. "Characterisation of a novel soybean candidate glutathione peroxidase/thioredoxin-dependent peroxidase in soybean exposed to osmotic/drought stress." University of the Western Cape, 2012. http://hdl.handle.net/11394/4643.

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>Magister Scientiae - MSc<br>Drought stress is a major contributor to reduced soybean crop yield and quality, this can however be mitigated by the plant’s antioxidant defence mechanisms. One group of antioxidant enzymes that are active in these defence mechanisms are glutathione peroxidases (GPXs). GPXs are antioxidant proteins which are able to reduce H2O2, a toxic reactive oxygen species which accumulates under stress conditions. This study aims at isolating the protein encoded by Glyma01g42840 and determining if it has Phospholipid hydroperoxidase glutathione peroxidase (PHGPX) and/or Thior
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Harthill, Jean Elizabeth. "N-glycosylation of horseradish peroxidase." Thesis, University of Oxford, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.292612.

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Pannell, Sarah Esme. "Structural determinants of peroxidase activities." Thesis, University of Sussex, 2011. http://sro.sussex.ac.uk/id/eprint/7463/.

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Horseradish peroxidase (HRP) is a robust enzyme with commercial applications as an immunodiagnostic reporter enzyme and in the catalysis of difficult chemical transformations. The commercial enzyme is still isolated from the roots of the horseradish plant Armoracia rusticana, and has been studied as a model haem enzyme system since the early 1940's. Following the development of methods to produce the active recombinant enzyme in E.coli (Smith et al., 1990) and completion of the crystallographic structure in 1997 (Gajhede et al., 1997) it has been possible to identify the structural requirement
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Knight, Simon Alexander Bowles 1961. "The use of anti-glutathione peroxidase antibodies in the study of selenium-dependent glutathione peroxidase." Thesis, The University of Arizona, 1988. http://hdl.handle.net/10150/276906.

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Liver glutathione peroxidase activity is affected by changes in selenium (Se) status. To investigate the effect of Se status on GSH-Px protein we prepared antibodies against rat liver GSH-Px and used them in an ELISA. The immunoreactivity of the anti-GSH-Px antibodies against GSH-Px was both tissue and species specific. When rats were depleted of Se, liver GSH-Px activity decreased exponentially to zero with a half-life of 2.8 d. Liver GSH-Px protein also decreased exponentially, but not to zero, with a longer half-life of 5.2 d. Dietary repletion of Se-deficient rats with 0.5 mg Se/kg diet in
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Books on the topic "I> Peroxidase"

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Dunford, H. Brian. Heme peroxidases. John Wiley, 1999.

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Silaghi-Dumitrescu, Radu. Horseradish peroxidase: A versatile catalyst, 2006. Transworld Research Network, 2006.

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Petrides, Petro E., and William M. Nauseef, eds. The Peroxidase Multigene Family of Enzymes. Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-642-58314-8.

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Hassan, Afaf Mahmoud. Glutathione peroxidase activity in aspirin-induced asthma. Universityof Manchester, 1995.

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Zerizer, Sakina. Comparative biochemical study of peroxidase assay systems. University of Salford, 1987.

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Biocatalysis based on heme peroxidases: Peroxidases as potential industrial biocatalysts. Springer-Verlag, 2010.

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Ohtaki, Sachiya. Selected papers of Professor Sachiya Ohtaki. s.n., 2002.

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Gómez, J. L. Soybeans, a peroxidase source for the biotreatment of effluents. Nova Science Publishers, 2010.

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Gómez, J. L., and J. L. Gómez. Soybeans, a peroxidase source for the biotreatment of effluents. Nova Science Publishers, 2010.

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Foote, Nicholas. Studies on the cytochrome c peroxidase of Ps. aeruginosa. University of East Anglia, 1985.

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Book chapters on the topic "I> Peroxidase"

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Stellmach, Bruno. "Peroxidase." In Bestimmungsmethoden Enzyme. Steinkopff, 1988. http://dx.doi.org/10.1007/978-3-642-93668-5_28.

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Schomburg, D., M. Salzmann, and D. Stephan. "Peroxidase." In Enzyme Handbook 7. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_142.

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Cai, Danying, and Ming Tien. "Lignin Peroxidase." In ACS Symposium Series. American Chemical Society, 1991. http://dx.doi.org/10.1021/bk-1991-0460.ch014.

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Wong, Dominic W. S. "Horseradish Peroxidase." In Food Enzymes. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4757-2349-6_11.

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Mittler, Ron, and Thomas L. Poulos. "Ascorbate Peroxidase." In Antioxidants and Reactive Oxygen Species in Plants. Blackwell Publishing Ltd, 2007. http://dx.doi.org/10.1002/9780470988565.ch4.

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Reddy, C. C., and G. A. Hamilton. "Glutathione Peroxidase." In Inorganic Reactions and Methods. John Wiley & Sons, Inc., 2007. http://dx.doi.org/10.1002/9780470145319.ch211.

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Schomburg, D., M. Salzmann, and D. Stephan. "NADH peroxidase." In Enzyme Handbook 7. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_137.

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Schomburg, D., M. Salzmann, and D. Stephan. "NADPH peroxidase." In Enzyme Handbook 7. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_138.

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Schomburg, D., M. Salzmann, and D. Stephan. "Iodide peroxidase." In Enzyme Handbook 7. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_143.

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Schomburg, D., M. Salzmann, and D. Stephan. "Glutathione peroxidase." In Enzyme Handbook 7. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_144.

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Conference papers on the topic "I> Peroxidase"

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Schaffer, W. M., and T. V. Bronnikova. "Modeling Peroxidase-Oxidase Interactions." In ASME 2011 Dynamic Systems and Control Conference and Bath/ASME Symposium on Fluid Power and Motion Control. ASMEDC, 2011. http://dx.doi.org/10.1115/dscc2011-5946.

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Reactive oxygen species (ROS) and peroxidase-oxidase (PO) reactions are Janus-faced contributors to cellular metabolism. At low concentrations, reactive oxygen species serve as signaling molecules; at high concentrations, as destroyers of proteins, lipids and DNA. Correspondingly, PO reactions are both sources and consumers of ROS. In the present paper, we study a well-tested model of the PO reaction based on horseradish peroxidase chemistry. Our principal predictions are these: 1. Under hypoxia, the PO reaction can emit pulses of hydrogen peroxide at apparently arbitrarily long intervals. 2.
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Mărîi, Liliana, Larisa Andronic, Svetlana Smerea, and Irina Erhan. "Dinamica răspunsului antioxidativ la tomatele cu diferit tip de interacțiune cu agentul viral." In International Scientific Symposium "Plant Protection – Achievements and Prospects". Institute of Genetics, Physiology and Plant Protection, Republic of Moldova, 2020. http://dx.doi.org/10.53040/9789975347204.70.

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The defensive response of 4 tomato genotypes to Tobacco Mosaic Virus or Tomato Aspermy Virus was evaluated according to 3 indices - peroxidase and catalase activities and hydrogen peroxide content. The response was differentiated according to the applied viral infection, the genotype and dynamics of the infection process. Particularities have been attested in the reaction of the antioxidative response at different stages of the pathogenesis - increasing or decreasing of the evaluated indices compared to the healthy control.
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NOZAKI, OSAMU, and HIROKO KAWAMOTO. "DETERMINATION OF HYDROGEN PEROXIDE BY MICRO - FLOW INJECTION – HORSERADISH PEROXIDASE CATALYZED “IMIDAZOLE CHEMILUMINESCENCE”." In Bioluminescence and Chemiluminescence - Progress and Current Applications - 12th International Symposium on Bioluminescence (BL) and Chemiluminescence (CL). WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776624_0075.

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Gaidamauskaite, E., and R. Baronas. "Modelling A Peroxidase-Based Fluorescent Biosensor." In 22nd Conference on Modelling and Simulation. ECMS, 2008. http://dx.doi.org/10.7148/2008-0152.

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Chang-Cheng Gao, Xian-Feng Zou, Qiong Wu, Xing Chen, Li-Hong Zhang, and Li-Na Chen. "A novel micromolecule glutathione peroxidase mimic." In 2011 International Symposium on Information Technology in Medicine and Education (ITME 2011). IEEE, 2011. http://dx.doi.org/10.1109/itime.2011.6132096.

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Sitter, Andrew J., Catherine M. Reczek, and James Terner. "Resonance Raman Spectroscopy Of Peroxidase Intermediates." In OE/LASE '89, edited by Fran Adar, James E. Griffiths, and Jeremy M. Lerner. SPIE, 1989. http://dx.doi.org/10.1117/12.951598.

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MAGLIA, GIOVANNI, and LARRY J. KRICKA. "EFFECT OF SOLVENTS AND POLYMERS ON THE BORONIC ACID ENHANCED PEROXIDASE - LUMINOL - PEROXIDE REACTION." In Proceedings of the 11th International Symposium. WORLD SCIENTIFIC, 2001. http://dx.doi.org/10.1142/9789812811158_0056.

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Leksin, I. Yu, C. C. Gorina, and F. V. Minibaeva. "Lichen peroxidase genes: cloning, sequencing, analysis activity." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-260.

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Bento, Tamyrys, Luis Rodrigues, Luiz Silva, et al. "Synthesis of Lophirone C using coconut peroxidase." In MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition. MDPI, 2018. http://dx.doi.org/10.3390/mol2net-04-05541.

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Laberge, Monique, and Istvan Kovesi. "Principal components analysis filters functionally significant peroxidase motions." In 2010 IEEE Symposium on Computational Intelligence in Bioinformatics and Computational Biology (CIBCB). IEEE, 2010. http://dx.doi.org/10.1109/cibcb.2010.5510723.

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Reports on the topic "I> Peroxidase"

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Arnold, Frances H. Expression and Directed Evolution of Peroxidase Enzymes. Defense Technical Information Center, 2000. http://dx.doi.org/10.21236/ada378502.

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Lagrimini, L. (Molecular characteristics of the lignin forming peroxidase). Office of Scientific and Technical Information (OSTI), 1990. http://dx.doi.org/10.2172/7138283.

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Lagrimini, L. M. The molecular characterization of the lignin-forming peroxidase. Office of Scientific and Technical Information (OSTI), 1992. http://dx.doi.org/10.2172/5445343.

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Stoyanova, Tsveta, Daniela Ivanova, Albena Alexandrova, and Stanislav Yanev. Interaction and Metabolism of N-Octylxanthate by Horseradish Peroxidase. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, 2019. http://dx.doi.org/10.7546/crabs.2019.04.06.

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Barstad, Louise. Purification and characterization of NADH oxidase and peroxidase from Lactobacillus casei. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.2785.

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Diamond, A. M., J. L. Murray, P. Dale, R. Tritz, and D. J. Grdina. The effects of selenium on glutathione peroxidase activity and radioprotection in mammalian cells. Office of Scientific and Technical Information (OSTI), 1995. http://dx.doi.org/10.2172/510356.

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Lagrimini, L. M. The molecular characterization of the lignin-forming peroxidase. Progress summary report, April 1, 1989--March 31, 1992. Office of Scientific and Technical Information (OSTI), 1992. http://dx.doi.org/10.2172/10135331.

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Beatty, Christopher, Joshua Kitner, Curtis Lajoie, Sean McClain, and Steve Potochnik. Advanced Recombinant Manganese Peroxidase for Biosynthesis of Lignin Bioproducts, Phase I Final Report, STTR Grant #: DE-SC0007503. Office of Scientific and Technical Information (OSTI), 2012. http://dx.doi.org/10.2172/1057291.

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Lagrimini, L. M. The molecular characterization of the lignin-forming peroxidase. Progress summary report, April 1, 1992--March 31, 1995. Office of Scientific and Technical Information (OSTI), 1995. http://dx.doi.org/10.2172/74118.

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Lagrimini, L. M. Molecular characterization of the lignin-forming peroxidase: Role in growth, development and response to stress. Progress summary report, April 1, 1993--March 31, 1994. Office of Scientific and Technical Information (OSTI), 1994. http://dx.doi.org/10.2172/10144262.

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