PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7852368-0 1995 Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Bromides 13-20 eosinophil peroxidase Homo sapiens 72-93 8825615-5 1996 The virucidal effect of eosinophils, PMA, and bromide under these conditions is inhibited by the peroxidase inhibitor azide and catalase, but not heated catalase or superoxide dismutase, implicating the EPO-H2O2-halide system. Bromides 46-53 eosinophil peroxidase Homo sapiens 203-206 8825615-7 1996 When the EPO concentration is suboptimal, virucidal activity is increased by bromide, iodide, and, in this instance, thiocyanate and the virucidal activity of the bromide-supplemented system is inhibited by azide and catalase. Bromides 77-84 eosinophil peroxidase Homo sapiens 9-12 8825615-7 1996 When the EPO concentration is suboptimal, virucidal activity is increased by bromide, iodide, and, in this instance, thiocyanate and the virucidal activity of the bromide-supplemented system is inhibited by azide and catalase. Bromides 163-170 eosinophil peroxidase Homo sapiens 9-12 10452808-8 1999 Although EPX can also oxidize bromide to generate HOBr, activities of MPO and EPX can be distinguished at different pHs. Bromides 30-37 eosinophil peroxidase Homo sapiens 9-12 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 eosinophil peroxidase Homo sapiens 105-126 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 eosinophil peroxidase Homo sapiens 20-41 1324677-9 1992 EPO, but not MPO, was partially protected against inactivation by adding physiologic levels of bromide along with chloride. Bromides 95-102 eosinophil peroxidase Homo sapiens 0-3 18516076-5 2008 KEY RESULTS: In the presence of plasma levels of bromide (Br-), melatonin inactivates EPO at two different points in the classic peroxidase cycle. Bromides 49-56 eosinophil peroxidase Homo sapiens 86-89 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 eosinophil peroxidase Homo sapiens 52-55 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 eosinophil peroxidase Homo sapiens 74-77 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 eosinophil peroxidase Homo sapiens 113-116 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 eosinophil peroxidase Homo sapiens 44-65 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 204-211 eosinophil peroxidase Homo sapiens 228-249 29400693-6 2018 EPO catalyzed oxidation of thiocyanate and bromide by H2O2 to generate oxidants that crosslink cysteine thiol groups and stiffen thiolated hydrogels. Bromides 43-50 eosinophil peroxidase Homo sapiens 0-3 25762223-13 2015 Only the chlorinating activity of EPO is efficiently inhibited by CP, while the capacity of EPO to oxidize bromide and thiocyanate practically does not depend on the presence of CP. Bromides 107-114 eosinophil peroxidase Homo sapiens 92-95 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 eosinophil peroxidase Homo sapiens 25-46 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 eosinophil peroxidase Homo sapiens 120-141 17209551-3 2007 The enzyme uses hydrogen peroxide (H2O2) and bromide (Br-), a preferred cosubstrate of EPO, to generate the cytotoxic oxidant hypobromous acid. Bromides 45-52 eosinophil peroxidase Homo sapiens 87-90 16166591-1 2006 In vivo, bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-)) compete for oxidation by eosinophil peroxidase (EPO) and H(2)O(2), yielding, respectively, HOBr, NO(2)., and HOSCN. Bromides 9-16 eosinophil peroxidase Homo sapiens 96-117 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. Bromides 217-224 eosinophil peroxidase Homo sapiens 141-162 16166591-1 2006 In vivo, bromide (Br(-)), nitrite (NO(2)(-)), and thiocyanate (SCN(-)) compete for oxidation by eosinophil peroxidase (EPO) and H(2)O(2), yielding, respectively, HOBr, NO(2)., and HOSCN. Bromides 9-16 eosinophil peroxidase Homo sapiens 119-122 11485572-5 2001 On the basis of these values thiocyanate is preferred 2.8-fold over bromide as a substrate for eosinophil peroxidase. Bromides 68-75 eosinophil peroxidase Homo sapiens 95-116 12643282-8 2003 Bromide was the preferred substrate for eosinophil peroxidase, and chloride was not appreciably used even at a 1000-fold molar excess. Bromides 0-7 eosinophil peroxidase Homo sapiens 40-61 11485572-11 2001 We conclude that at plasma concentrations of bromide (20-120 microM) and thiocyanate (20-100 microM), hypobromous acid and oxidation products of thiocyanate are produced by eosinophil peroxidase. Bromides 45-52 eosinophil peroxidase Homo sapiens 173-194 11329271-5 2001 Here, we show that EPO effectively uses plasma levels of bromide as a cosubstrate to brominate bases in nucleotides and double-stranded DNA, forming several stable novel brominated adducts. Bromides 57-64 eosinophil peroxidase Homo sapiens 19-22 11329272-0 2001 The eosinophil peroxidase-hydrogen peroxide-bromide system of human eosinophils generates 5-bromouracil, a mutagenic thymine analogue. Bromides 44-51 eosinophil peroxidase Homo sapiens 4-25