PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 18851713-1 2009 MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous acids. Bromides 59-66 myeloperoxidase Homo sapiens 0-3 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. Bromides 62-69 myeloperoxidase Homo sapiens 35-38 22718769-9 2012 Here the dye well reflected the different substrate specificities of myeloperoxidase and eosinophil peroxidase regarding chloride and bromide. Bromides 134-141 myeloperoxidase Homo sapiens 69-84 18851713-1 2009 MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous acids. Bromides 59-66 myeloperoxidase Homo sapiens 5-20 17604010-4 2007 This study was conducted to determine the effect physiological chloride concentration (140 mM) has on the formation of bromohydrins and lyso-PC from unsaturated PC upon treatment with the myeloperoxidase/hydrogen peroxide/bromide (MPO/H2O2/Br-) system using physiological bromide concentrations (20-100 microM). Bromides 272-279 myeloperoxidase Homo sapiens 231-234 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. Bromides 98-105 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. Bromides 98-105 myeloperoxidase Homo sapiens 38-41 17604010-4 2007 This study was conducted to determine the effect physiological chloride concentration (140 mM) has on the formation of bromohydrins and lyso-PC from unsaturated PC upon treatment with the myeloperoxidase/hydrogen peroxide/bromide (MPO/H2O2/Br-) system using physiological bromide concentrations (20-100 microM). Bromides 222-229 myeloperoxidase Homo sapiens 231-234 17604010-4 2007 This study was conducted to determine the effect physiological chloride concentration (140 mM) has on the formation of bromohydrins and lyso-PC from unsaturated PC upon treatment with the myeloperoxidase/hydrogen peroxide/bromide (MPO/H2O2/Br-) system using physiological bromide concentrations (20-100 microM). Bromides 272-279 myeloperoxidase Homo sapiens 188-203 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. Bromides 106-113 myeloperoxidase Homo sapiens 84-87 17604010-11 2007 The results indicate that at physiological levels of chloride and bromide, chloride promotes MPO-mediated formation of bromohydrins and lyso-PC in unsaturated phospholipids. Bromides 66-73 myeloperoxidase Homo sapiens 93-96 17141727-2 2007 Pretreatment of alpha1-antitrypsin with hypohalous acids HOCl and HOBr as well as with the myeloperoxidase-hydrogen peroxide-chloride (or bromide) system inactivated this proteinase. Bromides 138-145 myeloperoxidase Homo sapiens 91-106 17359937-8 2007 These findings are discussed with respect to the known crystal structure of MPO and its bromide complex as well as the known redox chemistry of its intermediates and substrates. Bromides 88-95 myeloperoxidase Homo sapiens 76-79 16125131-4 2006 We have investigated the ability of myeloperoxidase to produce hypobromous acid in the presence of physiological concentrations of chloride and bromide. Bromides 144-151 myeloperoxidase Homo sapiens 36-51 16288970-4 2006 Based on the published crystal structures of free MPO and its complexes with cyanide, bromide and thiocyanate as well as on sequence analysis and modeling, we critically discuss structure-function relationships. Bromides 86-93 myeloperoxidase Homo sapiens 50-53 16443167-4 2006 In the presence of chloride, bromide, and nitrite, the myeloperoxidase-hydrogen peroxide system caused an oxidation, bromination, and nitrosylation/nitration of eight amino acid residues of albumin as detected by fragment analysis of tryptic digests with matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry. Bromides 29-36 myeloperoxidase Homo sapiens 55-70 16125131-0 2006 Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Bromides 93-100 myeloperoxidase Homo sapiens 42-57 16125131-8 2006 Bromide, at physiological concentrations, promoted a dramatic increase in bromination of human serum albumin catalyzed by myeloperoxidase. Bromides 0-7 myeloperoxidase Homo sapiens 122-137 16125131-15 2006 We conclude that at physiological concentrations of chloride and bromide, hypobromous acid can be a major oxidant produced by myeloperoxidase. Bromides 65-72 myeloperoxidase Homo sapiens 126-141 9359420-1 1997 The neutrophil enzyme myeloperoxidase uses H2O2 to oxidize chloride, bromide, iodide and thiocyanate to their respective hypohalous acids. Bromides 69-76 myeloperoxidase Homo sapiens 22-37 11705390-0 2001 Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution. Bromides 79-86 myeloperoxidase Homo sapiens 6-21 11705390-5 2001 The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. Bromides 48-55 myeloperoxidase Homo sapiens 158-173 11705390-5 2001 The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. Bromides 241-248 myeloperoxidase Homo sapiens 158-173 10766826-4 2000 Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide. Bromides 66-73 myeloperoxidase Homo sapiens 50-65 10766826-4 2000 Determination of the x-ray crystal structure of a myeloperoxidase-bromide complex (r = 0.243, free r = 0.296) has shown that this chloride ion can be replaced by bromide. Bromides 162-169 myeloperoxidase Homo sapiens 50-65 10766826-6 2000 The bromide-binding site in the distal cavity appears to be the halide-binding site responsible for shifts in the Soret band of the absorption spectrum of myeloperoxidase. Bromides 4-11 myeloperoxidase Homo sapiens 155-170 12612415-0 2003 Modification by fluoride, bromide, iodide, thiocyanate and nitrite anions of reaction of a myeloperoxidase-H2O2-Cl- system with nucleosides. Bromides 26-33 myeloperoxidase Homo sapiens 91-106 10452808-0 1999 A myeloperoxidase-specific assay based upon bromide-dependent chemiluminescence of luminol. Bromides 44-51 myeloperoxidase Homo sapiens 2-17 9922160-0 1998 Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Bromides 54-61 myeloperoxidase Homo sapiens 12-27 9922160-9 1998 SCN- is shown to be most effective in shifting the system myeloperoxidase/hydrogen peroxide from the peroxidatic cycle to the halogenation cycle, whereas iodide is shown to be more effective than bromide which in turn is much more effective than chloride. Bromides 196-203 myeloperoxidase Homo sapiens 58-73 9359420-6 1997 The relative specificity constants for chloride, bromide and thiocyanate were 1:60:730 respectively, indicating that thiocyanate is by far the most favoured substrate for myeloperoxidase. Bromides 49-56 myeloperoxidase Homo sapiens 171-186 8131215-3 1994 Myeloperoxidase-dependent degradation of hyaluronic acid is inhibited by superoxide dismutase, desferrioxamine, iodide ion, bromide ion, mannitol, histidine and various antiinflammatory agents. Bromides 124-131 myeloperoxidase Homo sapiens 0-15 7852368-0 1995 Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Bromides 13-20 myeloperoxidase Homo sapiens 52-67 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. Bromides 69-76 myeloperoxidase Homo sapiens 0-15 8619607-1 1996 Eosinophil peroxidase and myeloperoxidase (MPO) catalyze the oxidation of bromide by hydrogen peroxide to produce hypobromous acid (HOBr). Bromides 74-81 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). Bromides 74-81 myeloperoxidase Homo sapiens 43-46 7852368-7 1995 In the presence of physiologic levels of both bromide (0.1 mM) and chloride (0.1 M), myeloperoxidase and eosinophil peroxidase produced mixtures of bromamines and chloramines containing 6 +/- 4% and 88 +/- 4% bromamine. Bromides 46-53 myeloperoxidase Homo sapiens 85-100 2838476-8 1988 The unique properties of eosinophil peroxidase are illustrated by the fact that at p2H 7.0 and with 100 microM bromide, eosinophil peroxidase generated 20 +/- 2% of the theoretical yield of singlet oxygen, whereas under identical conditions, myeloperoxidase and lactoperoxidase produced only 1.0 +/- 0.1% and -0.1 +/- 0.1%, respectively. Bromides 111-118 myeloperoxidase Homo sapiens 242-257 2154520-5 1990 Bromide or iodide caused up to a 7-fold increase in EPO activity and a 1.5-fold increase in MPO activity. Bromides 0-7 myeloperoxidase Homo sapiens 92-95 2154520-10 1990 Stimulation by bromide or iodide could be used to facilitate detection of EPO and to distinguish between MPO and EPO. Bromides 15-22 myeloperoxidase Homo sapiens 105-108 15104210-8 2004 In contrast, bromide can support H2O2/MPO/halide apoptosis, but is less potent than chloride and it has no effect in the presence of physiological levels of chloride. Bromides 13-20 myeloperoxidase Homo sapiens 38-41 2538427-5 1989 Since the relative halogenating behavior of eosinophil peroxidase and neutrophil myeloperoxidase in this bromide range is essentially identical to that of the cells, the specificity of eosinophils toward bromide is intrinsic to eosinophil peroxidase and not to any special cellular properties. Bromides 105-112 myeloperoxidase Homo sapiens 81-96 6272903-3 1981 When the non-bromide-containing cationic detergent cetyltrimethylammonium hydroxide (CTAOH) is used instead of CTAB, the eosinophils from MPO-deficient subjects are unable to decarboxylate L-alanine. Bromides 13-20 myeloperoxidase Homo sapiens 138-141 30082031-1 2018 Myeloperoxidase (MPO) is the enzyme of azurophilic granules of neutrophils, which catalyzes two electron oxidation of either chloride or bromide in the so-called "halogenating cycle". Bromides 137-144 myeloperoxidase Homo sapiens 0-15 30082031-1 2018 Myeloperoxidase (MPO) is the enzyme of azurophilic granules of neutrophils, which catalyzes two electron oxidation of either chloride or bromide in the so-called "halogenating cycle". Bromides 137-144 myeloperoxidase Homo sapiens 17-20