PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12071050-4 2002 Myeloperoxidase easily oxidizes thiocyanate to hypothiocyanate and Br- to HOBr, which are involved in protective reactions. hypobromous acid 74-78 myeloperoxidase Homo sapiens 0-15 12208372-1 2002 Eosinophil peroxidase and myeloperoxidase use hydrogen peroxide to produce hypobromous acid and hypochlorous acid. hypobromous acid 75-91 myeloperoxidase Homo sapiens 26-41 11697850-1 2001 Activated leukocytes generate the potent oxidants HOCl and HOBr via the formation of H(2)O(2) and the release of peroxidase enzymes (myeloperoxidase, eosinophil peroxidase). hypobromous acid 59-63 myeloperoxidase Homo sapiens 133-148 11425491-8 2001 Similar apoB modifications were observed with HOBr generated by MPO/H(2)O(2)/Br(-). hypobromous acid 46-50 myeloperoxidase Homo sapiens 64-67 1667454-2 1991 The chemiluminescence method was based on the detection of 1O2 generated by myeloperoxidase-catalyzed HOBr formation followed by the interaction of HOBr with H2O2 at pH 4.5. hypobromous acid 102-106 myeloperoxidase Homo sapiens 76-91 10452808-5 1999 The MPO-specific reaction is believed to proceed in two steps: (i) the enzymatic generation of hypobromous acid (HOBr) from KBr and H(2)O(2) at pH 5 and (ii) the spontaneous reaction of HOBr and H(2)O(2) with luminol to give a Br-CL signal. hypobromous acid 95-111 myeloperoxidase Homo sapiens 4-7 10452808-5 1999 The MPO-specific reaction is believed to proceed in two steps: (i) the enzymatic generation of hypobromous acid (HOBr) from KBr and H(2)O(2) at pH 5 and (ii) the spontaneous reaction of HOBr and H(2)O(2) with luminol to give a Br-CL signal. hypobromous acid 113-117 myeloperoxidase Homo sapiens 4-7 10452808-5 1999 The MPO-specific reaction is believed to proceed in two steps: (i) the enzymatic generation of hypobromous acid (HOBr) from KBr and H(2)O(2) at pH 5 and (ii) the spontaneous reaction of HOBr and H(2)O(2) with luminol to give a Br-CL signal. hypobromous acid 186-190 myeloperoxidase Homo sapiens 4-7 8619607-1 1996 Eosinophil peroxidase and myeloperoxidase (MPO) catalyze the oxidation of bromide by hydrogen peroxide to produce hypobromous acid (HOBr). hypobromous acid 132-136 myeloperoxidase Homo sapiens 26-41 8619607-1 1996 Eosinophil peroxidase and myeloperoxidase (MPO) catalyze the oxidation of bromide by hydrogen peroxide to produce hypobromous acid (HOBr). hypobromous acid 132-136 myeloperoxidase Homo sapiens 43-46 8619607-3 1996 In this study the equivalent reaction of HOBr, produced from MPO, bromide, and hydrogen peroxide, with oleic (18:1), linoleic (18:2), and arachidonic (20:4) acids has been investigated. hypobromous acid 41-45 myeloperoxidase Homo sapiens 61-64 2562426-6 1989 This suggested that, in the presence of MPO/H2O2 + Cl- + Br-, oxidation was due to HOBr from HOCl oxidation of Br- and/or oxidation of Br- by MPO/H2O2. hypobromous acid 83-87 myeloperoxidase Homo sapiens 40-43 34863835-1 2022 Previously we have shown that lactoferrin (LTF), a protein of secondary neutrophilic granules, can be efficiently modified by hypohalous acids (HOCl and HOBr), which are produced at high concentrations during inflammation and oxidative/halogenative stress by myeloperoxidase, an enzyme of azurophilic neutrophilic granules. hypobromous acid 153-157 myeloperoxidase Homo sapiens 259-274 15104210-5 2004 Hypobromous acid is likely a short-lived intermediate in this H2O2/MPO/bromide apoptosis, and reagent hypobromous acid and bromamines induce apoptosis in HL-60 cells. hypobromous acid 0-16 myeloperoxidase Homo sapiens 67-70 31015146-6 2019 The myeloperoxidase-derived oxidants hypochlorous acid, taurine chloramine, hypobromous acid, and hypothiocyanous acid, all at 10 muM, cross-linked calprotectin (5 muM) via reversible disulfide bonds. hypobromous acid 76-92 myeloperoxidase Homo sapiens 4-19 23685182-1 2013 Hypobromous acid (HOBr) is formed by eosinophil peroxidase and myeloperoxidase in the presence of H2O2, Cl(-), and Br(-) in the host defense system of humans, protecting against invading bacteria. hypobromous acid 0-16 myeloperoxidase Homo sapiens 63-78 25264081-8 2014 This dye is selectively oxidized by the MPO and EPO halogenation products hypochlorous and hypobromous acid. hypobromous acid 91-107 myeloperoxidase Homo sapiens 40-43 25438766-5 2014 Fourteen compounds were found to be potent inhibitors with IC50 values <1muM, suggesting these compounds could be considered as potential modulators of pro-oxidative tissue injury pertubated by the inflammatory MPO/H2O2/HOCl/HOBr system. hypobromous acid 228-232 myeloperoxidase Homo sapiens 214-217 24384524-1 2014 Halogenated lipids, proteins, and lipoproteins formed in reactions with myeloperoxidase (MPO)-derived hypochlorous acid (HOCl) and hypobromous acid (HOBr) can contribute to the regulation of functional activity of cells and serve as mediators of inflammation. hypobromous acid 149-153 myeloperoxidase Homo sapiens 72-87 24384524-1 2014 Halogenated lipids, proteins, and lipoproteins formed in reactions with myeloperoxidase (MPO)-derived hypochlorous acid (HOCl) and hypobromous acid (HOBr) can contribute to the regulation of functional activity of cells and serve as mediators of inflammation. hypobromous acid 149-153 myeloperoxidase Homo sapiens 89-92 28587811-2 2017 Here, we present the development of a sensitive and specific assay for determination of the halogenating enzymatic activity of MPO and EPO based on the electrophilic attack of HOCl and HOBr on aromatic ring of dansylglycine (DG). hypobromous acid 185-189 myeloperoxidase Homo sapiens 127-130 26456401-1 2015 At the sites of inflammation, hypohalous acids, such as hypochlorous acid and hypobromous acid (HOBr), are produced by myeloperoxidase. hypobromous acid 78-94 myeloperoxidase Homo sapiens 119-134 26456401-1 2015 At the sites of inflammation, hypohalous acids, such as hypochlorous acid and hypobromous acid (HOBr), are produced by myeloperoxidase. hypobromous acid 96-100 myeloperoxidase Homo sapiens 119-134 24632382-6 2014 This article reviews recent developments in our understanding of the cellular reactivity of hypochlorous acid, hypobromous acid, and hypothiocyanous acid, the major oxidants produced by myeloperoxidase under physiological conditions. hypobromous acid 111-127 myeloperoxidase Homo sapiens 186-201 23685182-1 2013 Hypobromous acid (HOBr) is formed by eosinophil peroxidase and myeloperoxidase in the presence of H2O2, Cl(-), and Br(-) in the host defense system of humans, protecting against invading bacteria. hypobromous acid 18-22 myeloperoxidase Homo sapiens 63-78 22982576-3 2012 Phagocyte-derived myeloperoxidase (MPO) utilizes chloride and bromide, in the presence of hydrogen peroxide (H(2)O(2)), to generate hypochlorous acid and hypobromous acid, potent oxidizing species that are known to kill invading pathogens. hypobromous acid 154-170 myeloperoxidase Homo sapiens 35-38 23719833-11 2013 Inhibition of myeloperoxidase involves paracetamol oxidation and concomitant decreased formation of halogenating oxidants (e.g. hypochlorous acid, hypobromous acid) that may be associated with multiple inflammatory pathologies including atherosclerosis and rheumatic diseases. hypobromous acid 147-163 myeloperoxidase Homo sapiens 14-29 23438648-5 2013 Another major participant of inflammatory response is the enzyme myeloperoxidase (MPO) which is secreted by neutrophils in the focus of inflammation and catalyzes formation of HOCl and HOBr. hypobromous acid 185-189 myeloperoxidase Homo sapiens 65-80 23438648-5 2013 Another major participant of inflammatory response is the enzyme myeloperoxidase (MPO) which is secreted by neutrophils in the focus of inflammation and catalyzes formation of HOCl and HOBr. hypobromous acid 185-189 myeloperoxidase Homo sapiens 82-85 20647044-11 2010 Our findings suggest that MPO produces hypobromous acid as well as hypochlorous acid in the airways of children with CF and that these oxidants are involved in the early pathogenesis of CF. hypobromous acid 39-55 myeloperoxidase Homo sapiens 26-29 21892922-2 2012 MPO catalyses the oxidation of Cl-, Br- and SCN- by H2O2 to generate the powerful oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) respectively. hypobromous acid 135-139 myeloperoxidase Homo sapiens 0-3 21241706-2 2011 Under inflammatory condition, cellular DNA is damaged by hypobromous acid, which is generated by myeloperoxidase and eosinophil peroxidase. hypobromous acid 57-73 myeloperoxidase Homo sapiens 97-112 20932962-4 2011 In contrast, chloro- and bromohydrins as well as dihalogenides are formed by the addition of HOCl or HOBr to the olefinic groups of the fatty acyl residues of lipids or under the influence of the enzyme myeloperoxidase (MPO) from Cl(-) and H(2)O(2). hypobromous acid 101-105 myeloperoxidase Homo sapiens 203-218 20932962-4 2011 In contrast, chloro- and bromohydrins as well as dihalogenides are formed by the addition of HOCl or HOBr to the olefinic groups of the fatty acyl residues of lipids or under the influence of the enzyme myeloperoxidase (MPO) from Cl(-) and H(2)O(2). hypobromous acid 101-105 myeloperoxidase Homo sapiens 220-223 17604010-8 2007 We attributed these effects to the involvement of HOBr arising from the reaction of MPO-derived HOCl with bromide rather than to the exchange of bromide with chlorine atoms of chlorohydrins or direct formation of HOBr by MPO. hypobromous acid 50-54 myeloperoxidase Homo sapiens 84-87 19788922-1 2010 The potent oxidants hypochlorous acid (HOCl) and hypobromous acid (HOBr) are produced extracellularly by myeloperoxidase, following release of this enzyme from activated leukocytes. hypobromous acid 67-71 myeloperoxidase Homo sapiens 105-120 18605737-2 2008 These lipids, in contrast to other phospholipids, have been reported to be targets of HOCl/HOBr generated by myeloperoxidase, with elevated levels of the products of these reactions (alpha-chloro/alpha-bromo aldehydes and unsaturated lysophospholipids) having been detected in human atherosclerotic lesions. hypobromous acid 91-95 myeloperoxidase Homo sapiens 109-124 17604010-1 2007 The leukocyte enzyme myeloperoxidase (MPO) is capable of catalyzing the oxidation of chloride and bromide ions, at physiological concentrations of these substrates, by hydrogen peroxide, generating hypochlorous acid (HOCl) and hypobromous acid (HOBr), respectively. hypobromous acid 245-249 myeloperoxidase Homo sapiens 21-36 17604010-1 2007 The leukocyte enzyme myeloperoxidase (MPO) is capable of catalyzing the oxidation of chloride and bromide ions, at physiological concentrations of these substrates, by hydrogen peroxide, generating hypochlorous acid (HOCl) and hypobromous acid (HOBr), respectively. hypobromous acid 245-249 myeloperoxidase Homo sapiens 38-41 19968966-1 2010 The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions. hypobromous acid 238-242 myeloperoxidase Homo sapiens 27-42 19968966-1 2010 The heme peroxidase enzyme myeloperoxidase (MPO) is released by activated neutrophils and monocytes, where it uses hydrogen peroxide (H(2)O(2)) to catalyze the production of the potent oxidants hypochlorous acid (HOCl), hypobromous acid (HOBr) and hypothiocyanous acid (HOSCN) from halide and pseudohalide (SCN(-)) ions. hypobromous acid 238-242 myeloperoxidase Homo sapiens 44-47 19968966-3 2010 It is shown here that acetaminophen (paracetamol), a phenol-based drug with analgesic and antipyretic actions, is an efficient inhibitor of HOCl and HOBr generation by isolated MPO-H(2)O(2)-halide systems. hypobromous acid 149-153 myeloperoxidase Homo sapiens 177-180 20408436-2 2010 Primary AH (HOCl and HOBr) are produced through oxidation of Cl- and Br- respectively by hydrogen peroxide catalyzed by myeloperoxidase or oesinophilic peroxidase. hypobromous acid 21-25 myeloperoxidase Homo sapiens 120-135 19708016-1 2009 Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing. hypobromous acid 0-16 myeloperoxidase Homo sapiens 73-88 19708016-1 2009 Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing. hypobromous acid 0-16 myeloperoxidase Homo sapiens 90-93 19708016-1 2009 Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing. hypobromous acid 18-22 myeloperoxidase Homo sapiens 73-88 19708016-1 2009 Hypobromous acid (HOBr) produced by both eosinophil peroxidase (EPO) and myeloperoxidase (MPO) is a stronger oxidant than HOCl, and is also essential for optimal and efficient microbial killing. hypobromous acid 18-22 myeloperoxidase Homo sapiens 90-93 17604010-8 2007 We attributed these effects to the involvement of HOBr arising from the reaction of MPO-derived HOCl with bromide rather than to the exchange of bromide with chlorine atoms of chlorohydrins or direct formation of HOBr by MPO. hypobromous acid 50-54 myeloperoxidase Homo sapiens 221-224 17604010-8 2007 We attributed these effects to the involvement of HOBr arising from the reaction of MPO-derived HOCl with bromide rather than to the exchange of bromide with chlorine atoms of chlorohydrins or direct formation of HOBr by MPO. hypobromous acid 213-217 myeloperoxidase Homo sapiens 221-224 17014424-1 2007 EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). hypobromous acid 120-124 myeloperoxidase Homo sapiens 32-35 17014424-1 2007 EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). hypobromous acid 120-124 myeloperoxidase Homo sapiens 37-52 17014424-1 2007 EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). hypobromous acid 126-142 myeloperoxidase Homo sapiens 32-35 17014424-1 2007 EPO (eosinophil peroxidase) and MPO (myeloperoxidase) are highly basic haem enzymes that can catalyse the production of HOBr (hypobromous acid). hypobromous acid 126-142 myeloperoxidase Homo sapiens 37-52 16125131-5 2006 In accord with previous studies, between pH 5 and 7, myeloperoxidase converted about 90% of available hydrogen peroxide to hypochlorous acid and the remainder to hypobromous acid. hypobromous acid 162-178 myeloperoxidase Homo sapiens 53-68 16125131-4 2006 We have investigated the ability of myeloperoxidase to produce hypobromous acid in the presence of physiological concentrations of chloride and bromide. hypobromous acid 63-79 myeloperoxidase Homo sapiens 36-51 16125131-15 2006 We conclude that at physiological concentrations of chloride and bromide, hypobromous acid can be a major oxidant produced by myeloperoxidase. hypobromous acid 74-90 myeloperoxidase Homo sapiens 126-141