PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 29400693-6 2018 EPO catalyzed oxidation of thiocyanate and bromide by H2O2 to generate oxidants that crosslink cysteine thiol groups and stiffen thiolated hydrogels. Hydrogen Peroxide 54-58 eosinophil peroxidase Homo sapiens 0-3 25193127-1 2014 Myeloperoxidase (MPO), lactoperoxidase (LPO) and eosinophil peroxidase (EPO) play a central role in oxidative damage in inflammatory disorders by utilizing hydrogen peroxide and halides/pseudo halides to generate the corresponding hypohalous acid. Hydrogen Peroxide 156-173 eosinophil peroxidase Homo sapiens 49-70 25193127-1 2014 Myeloperoxidase (MPO), lactoperoxidase (LPO) and eosinophil peroxidase (EPO) play a central role in oxidative damage in inflammatory disorders by utilizing hydrogen peroxide and halides/pseudo halides to generate the corresponding hypohalous acid. Hydrogen Peroxide 156-173 eosinophil peroxidase Homo sapiens 72-75 18516076-6 2008 First, it binds to EPO and forms an inactive complex, melatonin-EPO-Br, which restricts access of H2O2 to the catalytic site of the oxidation enzyme. Hydrogen Peroxide 98-102 eosinophil peroxidase Homo sapiens 64-67 18759245-15 2008 Eosinophil peroxidase catalyzes the H2O2 oxidation of Br- to HOBr, which N-brominates taurine to N-bromotaurine at its concentration of 15 mM in eosinophils. Hydrogen Peroxide 36-40 eosinophil peroxidase Homo sapiens 0-21 20974700-3 2011 When salbutamol was exposed to myeloperoxidase, eosinophil peroxidase or lactoperoxidase in the presence of hydrogen peroxide (H(2)O(2)) and nitrite (NO(2)(-)), both absorption spectroscopy and mass spectrometry indicated formation of a new metabolite with features expected for the nitrated drug. Hydrogen Peroxide 108-125 eosinophil peroxidase Homo sapiens 48-69 20501663-6 2010 Here we demonstrate that eosinophil peroxidase/H(2)O(2) is able to oxidize bisulfite, ultimately forming the sulfate anion radical (SO(4)()), and that these reactive intermediates can oxidize target proteins to protein radicals, thereby initiating protein oxidation. Hydrogen Peroxide 47-55 eosinophil peroxidase Homo sapiens 25-46 18047295-1 2007 Hypohalous acids are generated from the oxidation of halide ions by myeloperoxidase and eosinophil peroxidase in the presence of H2O2. Hydrogen Peroxide 129-133 eosinophil peroxidase Homo sapiens 88-109 16111649-1 2006 The formation of chloro- and bromohydrins from 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine following incubation with myeloperoxidase or eosinophil peroxidase in the presence of hydrogen peroxide, chloride and/or bromide was analysed by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Hydrogen Peroxide 182-199 eosinophil peroxidase Homo sapiens 141-162 17209551-3 2007 The enzyme uses hydrogen peroxide (H2O2) and bromide (Br-), a preferred cosubstrate of EPO, to generate the cytotoxic oxidant hypobromous acid. Hydrogen Peroxide 16-33 eosinophil peroxidase Homo sapiens 87-90 17209551-3 2007 The enzyme uses hydrogen peroxide (H2O2) and bromide (Br-), a preferred cosubstrate of EPO, to generate the cytotoxic oxidant hypobromous acid. Hydrogen Peroxide 35-39 eosinophil peroxidase Homo sapiens 87-90 17209551-6 2007 In the absence of NO, EPO-Fe(III) primarily converted to compound I and, upon H2O2 exhaustion, it decayed rapidly to the ferric form. Hydrogen Peroxide 78-82 eosinophil peroxidase Homo sapiens 22-25 16125131-1 2006 Myeloperoxidase and eosinophil peroxidase use hydrogen peroxide to oxidize halides and thiocyanate to their respective hypohalous acids. Hydrogen Peroxide 46-63 eosinophil peroxidase Homo sapiens 20-41 12960269-5 2003 In the presence of hydrogen peroxide and nitrite (NO2-; hereafter called EPO with substrates), EPO catalyzes the formation of nitrogen dioxide. Hydrogen Peroxide 19-36 eosinophil peroxidase Homo sapiens 73-76 12960269-5 2003 In the presence of hydrogen peroxide and nitrite (NO2-; hereafter called EPO with substrates), EPO catalyzes the formation of nitrogen dioxide. Hydrogen Peroxide 19-36 eosinophil peroxidase Homo sapiens 95-98 12208372-1 2002 Eosinophil peroxidase and myeloperoxidase use hydrogen peroxide to produce hypobromous acid and hypochlorous acid. Hydrogen Peroxide 46-63 eosinophil peroxidase Homo sapiens 0-21 12540536-7 2003 In contrast, EPO-treated bacteria frequently had cell wall lesions and eventually underwent lysis, either in the presence or in the absence of H(2)O(2). Hydrogen Peroxide 143-151 eosinophil peroxidase Homo sapiens 13-16 11589706-1 2001 The standard reduction potential of the redox couple compound I/native enzyme has been determined for human myeloperoxidase (MPO) and eosinophil peroxidase (EPO) at pH 7.0 and 25 degrees C. This was achieved by rapid mixing of peroxidases with either hydrogen peroxide or hypochlorous acid and measuring spectrophotometrically concentrations of the reacting species and products at equilibrium. Hydrogen Peroxide 251-268 eosinophil peroxidase Homo sapiens 157-160 11589706-2 2001 By using hydrogen peroxide, the standard reduction potential at pH 7.0 and 25 degrees C was 1.16 +/- 0.01 V for MPO and 1.10 +/- 0.01 V for EPO, independently of the concentration of hydrogen peroxide and peroxidases. Hydrogen Peroxide 9-26 eosinophil peroxidase Homo sapiens 140-143 11112545-3 2000 Addition of 1 equiv of hydrogen peroxide to native EPO leads to complete formation of compound I. Hydrogen Peroxide 23-40 eosinophil peroxidase Homo sapiens 51-54 11378533-2 2001 The enzymes myeloperoxidase and eosinophil peroxidase catalyze the reaction of H2 O2 with Cl to produce the reactive oxygen species HOCl. Hydrogen Peroxide 79-84 eosinophil peroxidase Homo sapiens 32-53 11329272-0 2001 The eosinophil peroxidase-hydrogen peroxide-bromide system of human eosinophils generates 5-bromouracil, a mutagenic thymine analogue. Hydrogen Peroxide 26-44 eosinophil peroxidase Homo sapiens 4-25 8492437-2 1993 Eosinophil peroxidase (EPO)+H2O2+halide system cause damage of respiratory epithelium, in vitro. Hydrogen Peroxide 28-32 eosinophil peroxidase Homo sapiens 0-21 8977530-11 1996 When EPO was combined with H2O2 and Br, 5.9 x 10(-9) mol/L EPO + 10(-5) mol/L H2O2 released two times more GM-CSF into the supernatants compared with control. Hydrogen Peroxide 27-31 eosinophil peroxidase Homo sapiens 59-62 8977530-11 1996 When EPO was combined with H2O2 and Br, 5.9 x 10(-9) mol/L EPO + 10(-5) mol/L H2O2 released two times more GM-CSF into the supernatants compared with control. Hydrogen Peroxide 78-82 eosinophil peroxidase Homo sapiens 5-8 8977530-11 1996 When EPO was combined with H2O2 and Br, 5.9 x 10(-9) mol/L EPO + 10(-5) mol/L H2O2 released two times more GM-CSF into the supernatants compared with control. Hydrogen Peroxide 78-82 eosinophil peroxidase Homo sapiens 59-62 7774640-0 1995 Human eosinophil peroxidase enhances tumor necrosis factor and hydrogen peroxide release by human monocyte-derived macrophages. Hydrogen Peroxide 63-80 eosinophil peroxidase Homo sapiens 6-27 7774640-3 1995 In this study, we report the effect of eosinophil peroxidase (EPO), a basic protein contained in eosinophils that binds to several cell types including macrophages, on tumor necrosis factor (TNF) production and hydrogen peroxide release by human monocyte-derived macrophages. Hydrogen Peroxide 211-228 eosinophil peroxidase Homo sapiens 39-60 7774640-3 1995 In this study, we report the effect of eosinophil peroxidase (EPO), a basic protein contained in eosinophils that binds to several cell types including macrophages, on tumor necrosis factor (TNF) production and hydrogen peroxide release by human monocyte-derived macrophages. Hydrogen Peroxide 211-228 eosinophil peroxidase Homo sapiens 62-65 7852368-2 1995 Myeloperoxidase and eosinophil peroxidase catalyzed the oxidation of bromide ion by hydrogen peroxide (H2O2) and produced a brominating agent that reacted with amine compounds to form bromamines, which are long-lived oxidants containing covalent nitrogen-bromine bonds. Hydrogen Peroxide 84-101 eosinophil peroxidase Homo sapiens 20-41 7852368-2 1995 Myeloperoxidase and eosinophil peroxidase catalyzed the oxidation of bromide ion by hydrogen peroxide (H2O2) and produced a brominating agent that reacted with amine compounds to form bromamines, which are long-lived oxidants containing covalent nitrogen-bromine bonds. Hydrogen Peroxide 103-107 eosinophil peroxidase Homo sapiens 20-41 11090610-2 2000 Myeloperoxidase (MPO), eosinophil peroxidase, and lactoperoxidase all catalytically consumed NO in the presence of the co-substrate hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 132-149 eosinophil peroxidase Homo sapiens 23-44 10090740-9 1999 Addition of primary amines (e.g., Nalpha-acetyllysine and taurine) to L-tyrosine exposed to either HOBr/OBr- or the EPO-H2O2-Br- system enhanced phenolic ring bromination, suggesting N-bromoamines are preferred brominating intermediates in these reactions. Hydrogen Peroxide 120-124 eosinophil peroxidase Homo sapiens 116-119 10090740-11 1999 Although both EPO and MPO could use Br- to halogenate protein tyrosine residues in vitro, only EPO effectively brominated the aromatic amino acid at physiological levels of halides and H2O2. Hydrogen Peroxide 185-189 eosinophil peroxidase Homo sapiens 95-98 8548780-1 1996 Certain human tumors are extensively infiltrated by eosinophils and contain extracellular deposits of eosinophil peroxidase, which uses hydrogen peroxide as a substrate to produce highly toxic hypohalous acids. Hydrogen Peroxide 136-153 eosinophil peroxidase Homo sapiens 102-123 7774640-4 1995 After incubation with EPO, the macrophages produced large amounts of TNF and displayed an enhanced phorbol 12-myristate 13-acetate-triggered hydrogen peroxide release. Hydrogen Peroxide 141-158 eosinophil peroxidase Homo sapiens 22-25 7774640-6 1995 The stimulatory effect of EPO on hydrogen peroxide release was insensitive to addition of exogenous catalase, a H2O2-degrading enzyme, suggesting that an extracellular catalytic activity of EPO was not involved. Hydrogen Peroxide 33-50 eosinophil peroxidase Homo sapiens 26-29 7961724-5 1994 Additionally, .OH was spin trapped following the addition of purified eosinophil peroxidase (EPO) to a cell-free O2-./H2O2 generating systems. Hydrogen Peroxide 118-122 eosinophil peroxidase Homo sapiens 70-91 7961724-5 1994 Additionally, .OH was spin trapped following the addition of purified eosinophil peroxidase (EPO) to a cell-free O2-./H2O2 generating systems. Hydrogen Peroxide 118-122 eosinophil peroxidase Homo sapiens 93-96 1849156-5 1991 Optimal assay conditions were as follows: pH 10.5, 10 microM hydrogen peroxide, 0.8 mM HVA and an incubation time of 120 min at 37 degrees C. Under these conditions the assay permits EPO activities as low as 0.025 guaiacol U/ml to be measured even in the presence of 0.175 guaiacol U/ml of MPO. Hydrogen Peroxide 61-78 eosinophil peroxidase Homo sapiens 183-186 2751158-11 1989 We hypothesize that the eosinophil peroxidase-hydrogen peroxide-halide system and major basic protein may injure the nasal epithelium in inflammatory conditions such as allergic and nonallergic eosinophilic rhinitis. Hydrogen Peroxide 46-63 eosinophil peroxidase Homo sapiens 24-45 3414778-4 1988 In the presence of 0.003% hydrogen peroxide, EPO + MBP was cytotoxic to five types of cells. Hydrogen Peroxide 26-43 eosinophil peroxidase Homo sapiens 45-48 3414778-6 1988 The toxicity of EPO + MBP is markedly enhanced by the presence of hydrogen peroxide. Hydrogen Peroxide 66-83 eosinophil peroxidase Homo sapiens 16-19 6420461-1 1984 It has been previously demonstrated that eosinophil peroxidase (EPO) when supplemented with hydrogen peroxide and a halide induces noncytotoxic mast cell degranulation. Hydrogen Peroxide 92-109 eosinophil peroxidase Homo sapiens 41-62 3029204-2 1987 To determine if the eosinophil peroxidase (EPO)-hydrogen peroxide (H2O2)-halide system could mediate this injury, we added human EPO, H2O2 (or glucose and glucose oxidase as a continuous source of H2O2), and various halides to monolayers of 51Cr-labeled human A549 and rat type II pneumocytes. Hydrogen Peroxide 48-65 eosinophil peroxidase Homo sapiens 20-41 3029204-9 1987 Catalase and azide substantially inhibited the lysis produced by the EPO-H2O2-halide system, suggesting that EPO-catalyzed products of halide oxidation mediated this form of injury. Hydrogen Peroxide 73-77 eosinophil peroxidase Homo sapiens 69-72 3029204-9 1987 Catalase and azide substantially inhibited the lysis produced by the EPO-H2O2-halide system, suggesting that EPO-catalyzed products of halide oxidation mediated this form of injury. Hydrogen Peroxide 73-77 eosinophil peroxidase Homo sapiens 109-112 3029204-11 1987 We hypothesize that the EPO-H2O2-halide system may injure the lung in asthma and eosinophilic pulmonary syndromes. Hydrogen Peroxide 28-32 eosinophil peroxidase Homo sapiens 24-27 6420461-1 1984 It has been previously demonstrated that eosinophil peroxidase (EPO) when supplemented with hydrogen peroxide and a halide induces noncytotoxic mast cell degranulation. Hydrogen Peroxide 92-109 eosinophil peroxidase Homo sapiens 64-67 6265355-7 1981 Under defined conditions (KI, 1.4 mM; H2O2, 0.18 mM; cetyltrimethylammonium bromide, 0.008% [wt/vol]; pH 6), the activity of eosinophil peroxidase could be measured in a mixed granulocyte suspension independently of myeloperoxidase. Hydrogen Peroxide 38-42 eosinophil peroxidase Homo sapiens 125-146 6309288-6 1983 In contrast, iodination was markedly augmented in MPO-deficient cells compared to normal cells after ingestion of zymosan coated with EPO (208 versus 70 nmole I-/10(7) monocytes/30 min; p less than 0.005), presumably reflecting the greater amounts of hydrogen peroxide formed by MPO-deficient cells. Hydrogen Peroxide 251-268 eosinophil peroxidase Homo sapiens 134-137 6696169-3 1984 The binding per se was not toxic to the organisms under our conditions, but EPO-coated schistosomula were rapidly killed when H2O2 and halide were added, under conditions in which uncoated schistosomula were unaffected. Hydrogen Peroxide 126-130 eosinophil peroxidase Homo sapiens 76-79 6696169-7 1984 This is compatible with the involvement of surface-bound EPO in an enzymatic attack on the organism, utilizing H2O2 generated by PMNs stimulated by adherence to antibody and complement-coated schistosomula. Hydrogen Peroxide 111-115 eosinophil peroxidase Homo sapiens 57-60 6273182-4 1981 The larvicidal effect was dependent on each component of the EPO/H2O2/Cl- system and could be prevented by using SO4(2-) instead of Cl-. Hydrogen Peroxide 65-69 eosinophil peroxidase Homo sapiens 61-64 678676-4 1978 This correlates with an inability of eosinophil peroxidase to catalyze the peroxidase-H2O2-CI--mediated decarboxylation of amino acids; in contrast, both eosinophil and neutrophil peroxidases showed similar capabilities to iodinate protein in vitro. Hydrogen Peroxide 86-90 eosinophil peroxidase Homo sapiens 37-58 7252407-7 1981 EPO release from eosinophils may contribute to this sequence of reactions, both by stimulation of H2O2-induced mast cell secretion and by combination with MCG to form a complex with augmented tumoricidal activity. Hydrogen Peroxide 98-102 eosinophil peroxidase Homo sapiens 0-3 6987310-4 1980 The MCG/EPO complex retained the capacity of the isolated EPO to catalyze the iodination reaction when supplemented with iodide, H2O2, and a protein acceptor and to kill microorganisms when supplemented with H2O2 and a halide (iodide, chloride). Hydrogen Peroxide 129-133 eosinophil peroxidase Homo sapiens 8-11 6987310-4 1980 The MCG/EPO complex retained the capacity of the isolated EPO to catalyze the iodination reaction when supplemented with iodide, H2O2, and a protein acceptor and to kill microorganisms when supplemented with H2O2 and a halide (iodide, chloride). Hydrogen Peroxide 129-133 eosinophil peroxidase Homo sapiens 58-61 6987310-4 1980 The MCG/EPO complex retained the capacity of the isolated EPO to catalyze the iodination reaction when supplemented with iodide, H2O2, and a protein acceptor and to kill microorganisms when supplemented with H2O2 and a halide (iodide, chloride). Hydrogen Peroxide 208-212 eosinophil peroxidase Homo sapiens 8-11 6987310-4 1980 The MCG/EPO complex retained the capacity of the isolated EPO to catalyze the iodination reaction when supplemented with iodide, H2O2, and a protein acceptor and to kill microorganisms when supplemented with H2O2 and a halide (iodide, chloride). Hydrogen Peroxide 208-212 eosinophil peroxidase Homo sapiens 58-61 6156983-1 1980 Eosinophil peroxidase (EPO) at relatively low levels (4-30 mU), when supplemented with H2O2 and a halide, induced mast cell degranulation. Hydrogen Peroxide 87-91 eosinophil peroxidase Homo sapiens 0-21 6156983-1 1980 Eosinophil peroxidase (EPO) at relatively low levels (4-30 mU), when supplemented with H2O2 and a halide, induced mast cell degranulation. Hydrogen Peroxide 87-91 eosinophil peroxidase Homo sapiens 23-26 6156983-6 1980 When the EPO level was increased to 100 mU, combination with H2O2- and iodide-induced cytotoxic histamine release as indicated by concomitant LDH release and ultrastructural evidence of cell disruption. Hydrogen Peroxide 61-65 eosinophil peroxidase Homo sapiens 9-12 6156983-9 1980 The mast cell granule (MCG)/EPO complex when supplemented with H2O2 and iodide was more effective than free EPO in the stimulation of mast cell secretion. Hydrogen Peroxide 63-67 eosinophil peroxidase Homo sapiens 28-31 6156983-10 1980 The stimulation of mast cell mediator release by the EPO-H2O2-halide system and the formation of MCG/EPO complexes with augmented cytotoxic activity may influence the adjacent inflammatory response. Hydrogen Peroxide 57-61 eosinophil peroxidase Homo sapiens 53-56 33295888-2 2021 Herein, we demonstrate the biodegradation of graphene oxide (GO) by recombinant eosinophil peroxidase (EPO) enzyme extracted from human eosinophils in the presence of a low concentration of hydrogen peroxide and NaBr. Hydrogen Peroxide 190-207 eosinophil peroxidase Homo sapiens 80-101 33295888-2 2021 Herein, we demonstrate the biodegradation of graphene oxide (GO) by recombinant eosinophil peroxidase (EPO) enzyme extracted from human eosinophils in the presence of a low concentration of hydrogen peroxide and NaBr. Hydrogen Peroxide 190-207 eosinophil peroxidase Homo sapiens 103-106