PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2155024-13 1990 In the presence of 5-aminosalicylic acid during the time interval in which the myeloperoxidase activity remained constant, a Km for H2O2 at pH 7.2 was determined of about 30 microM at 200 mM chloride. Chlorides 191-199 myeloperoxidase Homo sapiens 79-94 2157659-7 1990 Addition of H2O2 and chloride to MPO and C1q led to a complete inactivation of C1q, which could not be induced by H2O2 alone. Chlorides 21-29 myeloperoxidase Homo sapiens 33-36 2157659-8 1990 The hypochlorite, which is known to be generated during the reaction of MPO with H2O2 and chloride, exhibited a similar inactivating effect on C1q, which was prevented by an external source of methionine. Chlorides 90-98 myeloperoxidase Homo sapiens 72-75 2154520-8 1990 MPO catalyzes the oxidation of chloride to hypochlorus acid (HOCl), which also oxidized TMB, but chloride up to 20 mM had little effect on the assay. Chlorides 31-39 myeloperoxidase Homo sapiens 0-3 15104210-6 2004 We conclude that the physiologic concentrations of thiocyanate found in human plasma could modulate the cytototoxicity of H2O2 and its resulting highly toxic MPO-generated hypochlorous acid by competing with chloride for MPO. Chlorides 208-216 myeloperoxidase Homo sapiens 158-161 35513289-4 2022 It has previously been demonstrated that myeloperoxidase (MPO), which catalyzes formation of hypochlorous acid (HOCl) from hydrogen peroxide (H2O2) and chloride (Cl-), is enhanced in inflammatory diseases and could be a potent scavenger of NO. Chlorides 152-160 myeloperoxidase Homo sapiens 41-56 34640646-1 2021 Hypochlorous acid (HOCl) generates from the reaction between hydrogen peroxide and chloride ions via myeloperoxidase (MPO)-mediated in vivo. Chlorides 83-91 myeloperoxidase Homo sapiens 101-116 34640646-1 2021 Hypochlorous acid (HOCl) generates from the reaction between hydrogen peroxide and chloride ions via myeloperoxidase (MPO)-mediated in vivo. Chlorides 83-91 myeloperoxidase Homo sapiens 118-121 35620311-5 2022 MPO is the only human enzyme with the ability to produce hypochlorous acid (HOCl) at physiological chloride concentrations and HOCl-LDL epitopes were shown to be present inside atheromatous lesions making it a physiologically relevant model for the oxidation of LDL. Chlorides 99-107 myeloperoxidase Homo sapiens 0-3 35513289-4 2022 It has previously been demonstrated that myeloperoxidase (MPO), which catalyzes formation of hypochlorous acid (HOCl) from hydrogen peroxide (H2O2) and chloride (Cl-), is enhanced in inflammatory diseases and could be a potent scavenger of NO. Chlorides 152-160 myeloperoxidase Homo sapiens 58-61 35213685-6 2022 Prominent among PMN defense systems is their ability to generate hypochlorous acid (HOCl), a potent microbicide, by reacting oxidants generated by the NADPH oxidase with myeloperoxidase (MPO) released from azurophilic granules in the presence of chloride (Cl-). Chlorides 246-254 myeloperoxidase Homo sapiens 170-185 35213685-6 2022 Prominent among PMN defense systems is their ability to generate hypochlorous acid (HOCl), a potent microbicide, by reacting oxidants generated by the NADPH oxidase with myeloperoxidase (MPO) released from azurophilic granules in the presence of chloride (Cl-). Chlorides 246-254 myeloperoxidase Homo sapiens 187-190 2832092-7 1988 This data supports the notion that leucocyte myeloperoxidase may act to suppress the antiprotease screen afforded by alpha-1-PI by generating hypochlorous acid in the presence of chloride and respiratory burst-derived hydrogen peroxide, and in the microenvironment of lowered pH associated with degranulation. Chlorides 179-187 myeloperoxidase Homo sapiens 45-60 2844867-2 1988 It was found that exposure to MPO decreased adherence of many strains of oral streptococci to saliva-coated hydroxyapatite beads in the presence of exogenous H2O2 and chloride. Chlorides 167-175 myeloperoxidase Homo sapiens 30-33 2840860-8 1988 Iodination by MPO and H2O2 is stimulated by chloride due to the intermediate formation of hypochlorous acid (HOCl). Chlorides 44-52 myeloperoxidase Homo sapiens 14-17 2828362-8 1988 The H2O2-dependent portion of oxidation is mediated by myeloperoxidase-catalyzed oxidation of chloride to hypochlorous acid (HOCl) and oxidation of the reductants by HOCl. Chlorides 94-102 myeloperoxidase Homo sapiens 55-70 2546797-3 1989 This ratio was determined to be 1.2 for both the myeloperoxidase/H2O2/chloride system and the related compound NH2Cl. Chlorides 70-78 myeloperoxidase Homo sapiens 49-64 3030427-8 1987 This conclusion is supported by experiments which showed that formation of Compound III of myeloperoxidase by D-penicillamine depended on the chloride concentration. Chlorides 142-150 myeloperoxidase Homo sapiens 91-106 2822086-1 1987 The ligand binding properties of spleen myeloperoxidase, a peroxidase formerly called "the spleen green hemeprotein", were studied as functions of temperature and pH, using chloride and cyanide as exogenous ligands. Chlorides 173-181 myeloperoxidase Homo sapiens 40-55 3032796-3 1987 There appear to be three forms of MPO (MPO I, II, and III), all of which can kill this organism in the presence of H2O2 and chloride. Chlorides 124-132 myeloperoxidase Homo sapiens 34-37 3032796-3 1987 There appear to be three forms of MPO (MPO I, II, and III), all of which can kill this organism in the presence of H2O2 and chloride. Chlorides 124-132 myeloperoxidase Homo sapiens 39-42 3032796-9 1987 MPO bound to the high-avidity sites did not oxidize guaiacol but oxidized chloride, as detected by the chlorination of taurine. Chlorides 74-82 myeloperoxidase Homo sapiens 0-3 2854101-3 1987 Since myeloperoxidase (MPO), which is also active during the respiratory burst, produces hypochlorous acid (HOCl) (HOCl) in the presence of chloride ions (Cl-) and hydrogen peroxide (H2O2), this species has been investigated as a possible source of the DMPO-OH adduct. Chlorides 140-148 myeloperoxidase Homo sapiens 6-21 2854101-3 1987 Since myeloperoxidase (MPO), which is also active during the respiratory burst, produces hypochlorous acid (HOCl) (HOCl) in the presence of chloride ions (Cl-) and hydrogen peroxide (H2O2), this species has been investigated as a possible source of the DMPO-OH adduct. Chlorides 140-148 myeloperoxidase Homo sapiens 23-26 3022817-1 1986 N,N-Dimethyl-p-anisidine (DMA) was used as a substrate to differentiate between the direct, or chloride-independent, and the indirect, or chloride-dependent, pathways characteristic of myeloperoxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7). Chlorides 138-146 myeloperoxidase Homo sapiens 185-200 3024726-2 1986 In preliminary experiments, pre-exposure of either albumin or glomerular basement membrane to neutrophil myeloperoxidase with H2O2 and chloride increased their susceptibility to proteolysis 2-3-fold. Chlorides 135-143 myeloperoxidase Homo sapiens 105-120 2991128-3 1985 These findings indicate the involvement of the myeloperoxidase (MPO)-hydrogen peroxide (H2O2)-chloride (Cl-) system in the cytolytic process. Chlorides 94-102 myeloperoxidase Homo sapiens 47-62 3477210-5 1986 Myeloperoxidase will catalyse the peroxidation of the chloride ion but salivary peroxidase will not; the product of this in neutral solution is the hypochlorite ion, which is also a reactive oxidizing agent. Chlorides 54-62 myeloperoxidase Homo sapiens 0-15 2996923-4 1985 This hypothesis is supported by the prior observations that neutrophils are recruited in greater numbers into the lungs of smokers and that MPO (in the presence of H2O2 and chloride ion) oxidatively inactivates antiproteases of both the alveoli and the mucus-lined airways. Chlorides 173-181 myeloperoxidase Homo sapiens 140-143 2992450-0 1985 Production of the superoxide adduct of myeloperoxidase (compound III) by stimulated human neutrophils and its reactivity with hydrogen peroxide and chloride. Chlorides 148-156 myeloperoxidase Homo sapiens 39-54 2985447-0 1985 Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase. Chlorides 28-36 myeloperoxidase Homo sapiens 65-80 3011897-2 1986 The toxin activity of pneumolysin, as determined by lysis of 51Cr-labeled human erythrocytes, was destroyed on exposure to the neutrophil enzyme myeloperoxidase, hydrogen peroxide, and a halide (chloride or iodide). Chlorides 195-203 myeloperoxidase Homo sapiens 145-160 2989285-0 1985 The effect of chloride on the redox and EPR properties of myeloperoxidase. Chlorides 14-22 myeloperoxidase Homo sapiens 58-73 2989285-1 1985 Myeloperoxidase was purified from human polymorphonuclear leukocytes and the effect of chloride upon the EPR and potentiometric properties was studied. Chlorides 87-95 myeloperoxidase Homo sapiens 0-15 2989285-5 1985 Myeloperoxidase exhibited a rhombic high spin EPR signal which exhibited reduced rhombicity upon the binding of chloride. Chlorides 112-120 myeloperoxidase Homo sapiens 0-15 2989285-6 1985 Our results strongly suggest that chloride binds to the sixth coordination position of the chlorin iron in myeloperoxidase by replacing the water which is the sixth ligand in the resting state. Chlorides 34-42 myeloperoxidase Homo sapiens 107-122 2991128-3 1985 These findings indicate the involvement of the myeloperoxidase (MPO)-hydrogen peroxide (H2O2)-chloride (Cl-) system in the cytolytic process. Chlorides 94-102 myeloperoxidase Homo sapiens 64-67 6331509-7 1984 From their effects on the binding of cyanide to the enzyme it is concluded that chloride and thiocyanate bind to myeloperoxidase only when the acid/base group is protonated. Chlorides 80-88 myeloperoxidase Homo sapiens 113-128 6090506-7 1984 In contrast, the MPO-H2O2-chloride (Cl-) system was much less efficient. Chlorides 26-34 myeloperoxidase Homo sapiens 17-20 6381484-3 1984 Myeloperoxidase catalyzed the oxidation of chloride (Cl-) by H2O2 to yield hypochlorous acid (HOCl), which reacted with endogenous nitrogen compounds to yield derivatives containing nitrogen-chlorine (N-Cl) bonds. Chlorides 43-51 myeloperoxidase Homo sapiens 0-15 6331509-8 1984 The pH-dependence of the dissociation constant of the myeloperoxidase-chloride complex obtained from the spectral changes induced by chloride is the same as observed in the inhibition by chloride of the binding of cyanide. Chlorides 133-141 myeloperoxidase Homo sapiens 54-69 6331509-8 1984 The pH-dependence of the dissociation constant of the myeloperoxidase-chloride complex obtained from the spectral changes induced by chloride is the same as observed in the inhibition by chloride of the binding of cyanide. Chlorides 133-141 myeloperoxidase Homo sapiens 54-69 6321330-1 1984 Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) catalyse the formation of hypochlorite (OCl-) from chloride ions (OCl-) and hydrogen peroxide (H2O2). Chlorides 105-113 myeloperoxidase Homo sapiens 17-20 6331509-8 1984 The pH-dependence of the dissociation constant of the myeloperoxidase-chloride complex obtained from the spectral changes induced by chloride is the same as observed in the inhibition by chloride of the binding of cyanide. Chlorides 70-78 myeloperoxidase Homo sapiens 54-69 6195265-4 1983 This inhibition is due to a combination of the diminished release of myeloperoxidase and the scavenging of the luminol oxidant generated by the myeloperoxidase-H2O2-chloride system. Chlorides 165-173 myeloperoxidase Homo sapiens 69-84 6195265-5 1983 Although the polyanions heparin and dextran sulfate were effective in inhibiting luminol-dependent myeloperoxidase-H2O2-chloride chemiluminescence, the uncharged polysaccharide dextran T500 was without effect. Chlorides 120-128 myeloperoxidase Homo sapiens 99-114 6315067-1 1983 We investigated the effect of D-penicillamine on the ability of myeloperoxidase, purified from human leukocytes, to catalyse the oxidation of chloride ions to hypochlorite (HOCl) in the presence of H2O2. Chlorides 142-150 myeloperoxidase Homo sapiens 64-79 6315067-2 1983 It is shown that, due to the interaction of D-penicillamine with both myeloperoxidase itself and HOCl, the chlorinating activity of myeloperoxidase in the presence of H2O2 and chloride ions is prevented. Chlorides 176-184 myeloperoxidase Homo sapiens 70-85 6315067-2 1983 It is shown that, due to the interaction of D-penicillamine with both myeloperoxidase itself and HOCl, the chlorinating activity of myeloperoxidase in the presence of H2O2 and chloride ions is prevented. Chlorides 176-184 myeloperoxidase Homo sapiens 132-147 6195265-4 1983 This inhibition is due to a combination of the diminished release of myeloperoxidase and the scavenging of the luminol oxidant generated by the myeloperoxidase-H2O2-chloride system. Chlorides 165-173 myeloperoxidase Homo sapiens 144-159 6292181-0 1982 A kinetic analysis of the interaction of human myeloperoxidase with hydrogen peroxide, chloride ions, and protons. Chlorides 87-95 myeloperoxidase Homo sapiens 47-62 6301581-4 1983 Myeloperoxidase (MPO) in the ID-PMN population showed increased sensitivity to inhibition by 3-amino-1,2,4-triazole, and HD-PMN exhibited a 2-3-fold increase in chloride and iodide oxidation per unit of MPO activity compared to ID-PMN. Chlorides 161-169 myeloperoxidase Homo sapiens 0-15 6301581-4 1983 Myeloperoxidase (MPO) in the ID-PMN population showed increased sensitivity to inhibition by 3-amino-1,2,4-triazole, and HD-PMN exhibited a 2-3-fold increase in chloride and iodide oxidation per unit of MPO activity compared to ID-PMN. Chlorides 161-169 myeloperoxidase Homo sapiens 17-20 6308055-2 1983 Stimulation of neutrophil oxygen (O2) metabolism with phorbol myristate acetate or opsonized zymosan resulted in production of hydrogen peroxide (H2O2), myeloperoxidase-catalyzed oxidation of chloride (C1-) to hypochlorous acid (HOC1), and the reaction of HOC1 with the added compounds to yield nitrogen-chlorine (N-C1) derivatives. Chlorides 192-200 myeloperoxidase Homo sapiens 153-168 6295926-8 1983 Under the experimental conditions employed, PMA-activated neutrophils incubated with BCNU-treated Raji cells became cytotoxic also in the presence of the chloride ion alone as myeloperoxidase co-factor. Chlorides 154-162 myeloperoxidase Homo sapiens 176-191 6286728-2 1982 The model hydrogen peroxide-myeloperoxidase-chloride system is capable of generating the powerful oxidant hypochlorous acid, which can be quantitated by trapping the generated species with the beta-amino acid, taurine. Chlorides 44-52 myeloperoxidase Homo sapiens 28-43 6286728-4 1982 Using this system, purified myeloperoxidase in the presence of chloride and taurine converted stoichiometric quantities of hydrogen peroxide to taurine chloramine. Chlorides 63-71 myeloperoxidase Homo sapiens 28-43 6286728-11 1982 Thus, it appears that stimulated human neutrophils can utilize the hydrogen peroxide-myeloperoxidase-chloride system to generate taurine chloramine. Chlorides 101-109 myeloperoxidase Homo sapiens 85-100 6955794-8 1982 When hypochlorous acid (HOCl)-considered to be a natural product of the interaction of myeloperoxidase, H(2)O(2), and chloride ion-was formed chemically and allowed to react with LTC(4), the resulting products were indistinguishable by UV and HPLC analyses from the doublet II and doublet III metabolites of LTC(4). Chlorides 118-126 myeloperoxidase Homo sapiens 87-102 6295461-1 1982 Myeloperoxidase-catalyzed oxidation of chloride (Cl-) to hypochlorous acid (HOCl) resulted in formation of mono- and dichloramine derivatives (RNHCl and RNCl2) of primary amines. Chlorides 39-47 myeloperoxidase Homo sapiens 0-15 6258635-8 1981 Myeloperoxidase, in the presence of hydrogen peroxide and chloride ion, and no other substrate, autoinactivates. Chlorides 58-66 myeloperoxidase Homo sapiens 0-15 6276438-8 1982 Hypochlorous acid scavengers prevented CEM destruction by the glucose oxidase-myeloperoxidase-chloride system but neither hydroxyl radical nor singlet oxygen scavengers had any protective effect. Chlorides 94-102 myeloperoxidase Homo sapiens 78-93 6276438-10 1982 Based on these observations we propose that human monocytes or granulocytes can utilize the hydrogen peroxide-myeloperoxidase-chloride system to generate hypochlorous acid or species of similar reactivity as a potential mediator of CEM destruction. Chlorides 126-134 myeloperoxidase Homo sapiens 110-125 6253528-10 1980 In the case of PMA-stimulated polymorphonuclear leukocytes or monocytes, extracellular myeloperoxidase may have also played a role in alpha(1)-Pi inactivation since serum EIC was partly protected by azide, cyanide, or the depletion of extracellular chloride. Chlorides 249-257 myeloperoxidase Homo sapiens 87-102 6260684-9 1981 A sample of a very highly purified human myeloperoxidase functioned in the presence of hydrogen peroxide and either iodide or chloride to prevent germination of both blastospores and conidiospores. Chlorides 126-134 myeloperoxidase Homo sapiens 41-56 6244848-2 1980 The reaction of myeloperoxidase with fluoride, chloride and azide has been studied by EPR. Chlorides 47-55 myeloperoxidase Homo sapiens 16-31 6244848-9 1980 Upon addition of chloride or fluoride to low-spin azido-myeloperoxidase this compound is converted into the high-spin chlorido- or fluorido-myeloperoxidase. Chlorides 17-25 myeloperoxidase Homo sapiens 56-71 6244848-9 1980 Upon addition of chloride or fluoride to low-spin azido-myeloperoxidase this compound is converted into the high-spin chlorido- or fluorido-myeloperoxidase. Chlorides 17-25 myeloperoxidase Homo sapiens 140-155 182702-4 1976 Myeloperoxidase isolated from human leukocytes is cytotoxic when combined with H2O2 and chloride. Chlorides 88-96 myeloperoxidase Homo sapiens 0-15 36154-5 1979 Chloride competed with cyanide for binding at the active site of myeloperoxidase. Chlorides 0-8 myeloperoxidase Homo sapiens 65-80 225142-2 1978 After phagocytosis, MPO is released into the phagosome from adjacent granules where it interacts with H2O2 generated either by leukocytic or microbial metabolism and a halide such as chloride or iodide to form agents toxic to the ingested organisms. Chlorides 183-191 myeloperoxidase Homo sapiens 20-23 1120184-4 1975 Myeloperoxidase was effective with either chloride or iodide as the halide, while lastoperoxidase was effective with iodide but not chloride. Chlorides 42-50 myeloperoxidase Homo sapiens 0-15 170101-4 1975 The myeloperoxidase obtained from neutrophils catalyzes chlorination of protein (bovine serum albumin) and bacteria (Staphylococcus epidermidis) in the presence of hydrogen peroxide and chloride. Chlorides 186-194 myeloperoxidase Homo sapiens 4-19 1173052-1 1975 Erythrocytes are hemolyzed by myeloperoxidase, an H2O2-generating system (glucose + glucose oxidase; hypoxanthine + xanthine oxidase) and an oxidizable cofactor (chloride, iodide, thyroxine, triiodothyronine). Chlorides 162-170 myeloperoxidase Homo sapiens 30-45 4717124-2 1973 Myeloperoxidase, in amounts equivalent to 1.5 x 10(6) neutrophils, readily replaces lactoperoxidase, and allows the substitution of the iodide ion by chloride. Chlorides 150-158 myeloperoxidase Homo sapiens 0-15 33539947-2 2021 In the presence of chloride ions and hydrogen peroxide (H2O2), MPO forms the oxidant hypochlorous acid (HOCl). Chlorides 19-27 myeloperoxidase Homo sapiens 63-66 16557740-4 1970 Since we had previously found that myeloperoxidase (MPO), a lysosomal enzyme of human neutrophils and monocytes, exerted fungicidal activity against Candida albicans when combined with H(2)O(2) and chloride or iodide, the effects of these substances on A. fumigatus spores were examined. Chlorides 198-206 myeloperoxidase Homo sapiens 35-50 16557740-4 1970 Since we had previously found that myeloperoxidase (MPO), a lysosomal enzyme of human neutrophils and monocytes, exerted fungicidal activity against Candida albicans when combined with H(2)O(2) and chloride or iodide, the effects of these substances on A. fumigatus spores were examined. Chlorides 198-206 myeloperoxidase Homo sapiens 52-55 33631301-1 2021 Myeloperoxidase (MPO) is released by activated immune cells and forms the oxidants hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN) from the competing substrates chloride and thiocyanate. Chlorides 171-179 myeloperoxidase Homo sapiens 0-15 33631301-1 2021 Myeloperoxidase (MPO) is released by activated immune cells and forms the oxidants hypochlorous acid (HOCl) and hypothiocyanous acid (HOSCN) from the competing substrates chloride and thiocyanate. Chlorides 171-179 myeloperoxidase Homo sapiens 17-20 33350832-6 2021 Conclusions point to the innate oxidizing nature of MPO with the ester and sulfonium linkages hiking up the reactivity to enable chloride oxidation. Chlorides 129-137 myeloperoxidase Homo sapiens 52-55 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". Chlorides 125-133 myeloperoxidase Homo sapiens 0-15 33007547-1 2020 Myeloperoxidase (MPO) is a heme peroxidase found in neutrophils, monocytes and macrophages that efficiently catalyzes the oxidation of endogenous chloride into hypochlorous acid for antimicrobial activity. Chlorides 146-154 myeloperoxidase Homo sapiens 0-15 33007547-1 2020 Myeloperoxidase (MPO) is a heme peroxidase found in neutrophils, monocytes and macrophages that efficiently catalyzes the oxidation of endogenous chloride into hypochlorous acid for antimicrobial activity. Chlorides 146-154 myeloperoxidase Homo sapiens 17-20 32508671-4 2020 Activation of MPO can catalyze the reaction of chloride and H2O2 to produce HOCl. Chlorides 47-55 myeloperoxidase Homo sapiens 14-17 30531966-6 2019 This revealed that phagosome-lysosome fusion was essential not only for phagosome acidification, but also for providing the chloride necessary for myeloperoxidase activity. Chlorides 124-132 myeloperoxidase Homo sapiens 147-162 31103890-3 2019 Myeloperoxidase catalyzes the generation of hypochlorous acid (HOCl) from the reaction of hydrogen peroxide (H2O2) and chloride (Cl-). Chlorides 119-127 myeloperoxidase Homo sapiens 0-15 31238865-4 2019 Incubation of both proteins with hypochlorite (NaOCl) or catalytically active MPO (MPO + H2O2), which synthesizes hypochlorous acid (HOCl) in the presence of chloride ions, resulted in the quenching of protein tryptophan fluorescence. Chlorides 158-166 myeloperoxidase Homo sapiens 78-81 31238865-4 2019 Incubation of both proteins with hypochlorite (NaOCl) or catalytically active MPO (MPO + H2O2), which synthesizes hypochlorous acid (HOCl) in the presence of chloride ions, resulted in the quenching of protein tryptophan fluorescence. Chlorides 158-166 myeloperoxidase Homo sapiens 83-86 29394241-7 2019 Our data provide proof-of-principle that 2-ClPA and 2-ClHDA induce powerful proinflammatory responses both in vitro and in vivo, suggesting the possibility that these chlorinated lipid products of the MPO/ hydrogen peroxide /chloride system may contribute to inflammation noted in neutrophil-dependent, myeloperoxidase-mediated pathologic states such as ischemia/reperfusion, hemorrhagic shock, and sepsis. Chlorides 225-233 myeloperoxidase Homo sapiens 201-204 30118829-8 2018 Conversely, uric acid significantly decreased the levels of HOCl, probably because of the competition with chloride by the catalysis of myeloperoxidase. Chlorides 107-115 myeloperoxidase Homo sapiens 136-151 30206371-1 2018 Phagocytes destroy ingested microbes by producing hypochlorous acid (HOCl) from chloride ions (Cl-) and hydrogen peroxide within phagolysosomes, using the enzyme myeloperoxidase. Chlorides 80-88 myeloperoxidase Homo sapiens 162-177 29739865-4 2018 During neutrophil activation, MPO is released and activated to convert hydrogen peroxide and chloride to hypochlorous acid (HOCl). Chlorides 93-101 myeloperoxidase Homo sapiens 30-33 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". Chlorides 125-133 myeloperoxidase Homo sapiens 17-20 30082031-2 2018 Interaction of hydrogen peroxide with MPO in the presence of chloride ions leads to formation of hypochlorous acid (HOCl). Chlorides 61-69 myeloperoxidase Homo sapiens 38-41 28115520-1 2017 Neutrophil myeloperoxidase (MPO) catalyzes the H2O2-dependent oxidation of chloride anion to generate hypochlorous acid, a potent antimicrobial agent. Chlorides 75-89 myeloperoxidase Homo sapiens 11-26 29510342-8 2018 Our data show that uric acid impairs the killing activity of dHL-60 cells likely by competing with chloride by myeloperoxidase catalysis, decreasing HOCl production. Chlorides 99-107 myeloperoxidase Homo sapiens 111-126 29247550-1 2018 Hypochlorous acid (HOCl) is a potent cytotoxic oxidant generated by the enzyme myeloperoxidase (MPO) in the presence of hydrogen peroxide (H2 O2 ) and chloride (Cl- ). Chlorides 151-159 myeloperoxidase Homo sapiens 79-94 29247550-1 2018 Hypochlorous acid (HOCl) is a potent cytotoxic oxidant generated by the enzyme myeloperoxidase (MPO) in the presence of hydrogen peroxide (H2 O2 ) and chloride (Cl- ). Chlorides 151-159 myeloperoxidase Homo sapiens 96-99 29358899-7 2017 In vitro experiments using model peptides, in-solution oxidation, and click chemistry demonstrated that hypochlorous acid produced by the myeloperoxidase - hydrogen peroxide - chloride system could be responsible for these and other, more commonly observed modifications. Chlorides 176-184 myeloperoxidase Homo sapiens 138-153 29258826-4 2018 We have developed an assay for myeloperoxidase activity that includes its major physiological substrates - chloride, thiocyanate, tyrosine, and urate. Chlorides 107-115 myeloperoxidase Homo sapiens 31-46 28115520-1 2017 Neutrophil myeloperoxidase (MPO) catalyzes the H2O2-dependent oxidation of chloride anion to generate hypochlorous acid, a potent antimicrobial agent. Chlorides 75-89 myeloperoxidase Homo sapiens 28-31 27013775-1 2016 Myeloperoxidase is an inflammatory enzyme that generates reactive hypochlorous acid in the presence of hydrogen peroxide and chloride ion. Chlorides 125-133 myeloperoxidase Homo sapiens 0-15 28035220-2 2016 Neutrophils are the predominant white blood cells in circulation when stimulated; they discharge the abundant myeloperoxidase (MPO) enzyme that uses hydrogen peroxide to oxidize chloride for killing ingested bacteria. Chlorides 178-186 myeloperoxidase Homo sapiens 110-125 28035220-2 2016 Neutrophils are the predominant white blood cells in circulation when stimulated; they discharge the abundant myeloperoxidase (MPO) enzyme that uses hydrogen peroxide to oxidize chloride for killing ingested bacteria. Chlorides 178-186 myeloperoxidase Homo sapiens 127-130 27461359-14 2017 This correlation is assumed to be due to involvement of myeloperoxidase which catalyzes the formation of hypochlorite (-OCl) from chloride and hydrogen peroxide. Chlorides 130-138 myeloperoxidase Homo sapiens 56-71 27343172-1 2016 Human myeloperoxidase (MPO) uses chloride and thiocyanate as physiological substrates at neutral pH. Chlorides 33-41 myeloperoxidase Homo sapiens 6-21 27343172-1 2016 Human myeloperoxidase (MPO) uses chloride and thiocyanate as physiological substrates at neutral pH. Chlorides 33-41 myeloperoxidase Homo sapiens 23-26 25614581-9 2016 These results demonstrate the ability of MPO/H2O2/chloride ion system to oxidize DBAN to CN- and provide insight for the elucidation of DBAN chronic toxicity. Chlorides 50-58 myeloperoxidase Homo sapiens 41-44 25688920-1 2015 Myeloperoxidase (MPO) is expressed by myeloid cells for the purpose of catalyzing the formation of hypochlorous acid, from chloride ions and reaction with a hydrogen peroxide-charged heme covalently bound to the enzyme. Chlorides 123-131 myeloperoxidase Homo sapiens 0-15 25731855-2 2015 We addressed the question whether (i) the interaction of myeloperoxidase (MPO, an enzyme generating hypochlorous acid from hydrogen peroxide and chloride ions) with peroxynitrite affects the clearance of peroxynitrite, and (ii) if peroxynitrite could modulate the chlorinating activity of MPO. Chlorides 145-153 myeloperoxidase Homo sapiens 57-72 25731855-2 2015 We addressed the question whether (i) the interaction of myeloperoxidase (MPO, an enzyme generating hypochlorous acid from hydrogen peroxide and chloride ions) with peroxynitrite affects the clearance of peroxynitrite, and (ii) if peroxynitrite could modulate the chlorinating activity of MPO. Chlorides 145-153 myeloperoxidase Homo sapiens 74-77 25835505-6 2015 These include competition with chloride, the natural co-substrate; switching the MPO activity from a two electron oxidation to a one electron pathway causing the buildup of the inactive Compound II, and its subsequent decay to MPO-Fe(III) instead of generating HOCl; binding to MPO above the heme iron, thereby preventing the access of H2O2 to the catalytic site of the enzyme; and direct scavenging of HOCl. Chlorides 31-39 myeloperoxidase Homo sapiens 81-84 25688920-1 2015 Myeloperoxidase (MPO) is expressed by myeloid cells for the purpose of catalyzing the formation of hypochlorous acid, from chloride ions and reaction with a hydrogen peroxide-charged heme covalently bound to the enzyme. Chlorides 123-131 myeloperoxidase Homo sapiens 17-20 25460734-4 2014 Using the antibody, we observed that the chloride ion, the predominant physiological substrate for myeloperoxidase in vivo, is not competitive toward the enzyme catalyzed serotonin oxidation process, suggesting that serotonin is a plausible physiological substrate for the enzyme in vivo. Chlorides 41-49 myeloperoxidase Homo sapiens 99-114 25260666-7 2014 It could be demonstrated that the double bonds of the fatty acid hydroperoxides are the major target of HOCl, present either as reagent or formed by the myeloperoxidase-hydrogen peroxide-chloride system. Chlorides 187-195 myeloperoxidase Homo sapiens 153-168 25050609-2 2014 MPO uses H2O2 to generate oxidants including HOCl and HOSCN, from chloride and thiocyanate (SCN(-)) ions, respectively. Chlorides 66-74 myeloperoxidase Homo sapiens 0-3 24844117-4 2014 The most rapid and complete antimicrobial action by human neutrophils against many organisms relies on the combined efforts of the azurophilic granule protein myeloperoxidase and hydrogen peroxide from the NADPH oxidase to oxidize chloride, thereby generating hypochlorous acid and a host of downstream reaction products. Chlorides 231-239 myeloperoxidase Homo sapiens 159-174 24534704-1 2014 Oxidation of LDL by the myeloperoxidase (MPO)-H2O2-chloride system is a key event in the development of atherosclerosis. Chlorides 51-59 myeloperoxidase Homo sapiens 24-39 24534704-1 2014 Oxidation of LDL by the myeloperoxidase (MPO)-H2O2-chloride system is a key event in the development of atherosclerosis. Chlorides 51-59 myeloperoxidase Homo sapiens 41-44 24534704-5 2014 Using MS, we further analyzed in vitro modifications of apoB-100 by hypochlorous acid (HOCl) generated by the MPO-H2O2-chloride system or added as a reagent. Chlorides 119-127 myeloperoxidase Homo sapiens 110-113 24534704-7 2014 Furthermore, differences were observed between LDL oxidized by reagent HOCl or HOCl generated by the MPO-H2O2-chloride system. Chlorides 110-118 myeloperoxidase Homo sapiens 101-104 25283359-2 2014 The probe shows high selectivity and sensitivity toward HOCl under best working conditions of myeloperoxidase by which HOCl can be generated from hydrogen peroxide and chloride. Chlorides 168-176 myeloperoxidase Homo sapiens 94-109 24497481-1 2014 Hypochlorous acid (HOCl), a reactive oxygen species (ROS) produced by myeloperoxidase (MPO) enzyme-mediated peroxidation of chloride ions, acts as a key microbicidal agent in immune systems. Chlorides 124-132 myeloperoxidase Homo sapiens 70-85 24497481-1 2014 Hypochlorous acid (HOCl), a reactive oxygen species (ROS) produced by myeloperoxidase (MPO) enzyme-mediated peroxidation of chloride ions, acts as a key microbicidal agent in immune systems. Chlorides 124-132 myeloperoxidase Homo sapiens 87-90 24497481-7 2014 More importantly, RBH1-UCNPs could be used for the ratiometric UCL visualization of HOCl released by MPO-mediated peroxidation of chloride ions in living cells. Chlorides 130-138 myeloperoxidase Homo sapiens 101-104 24915973-9 2014 This compound is only catalyzed by myeloperoxidase in the presence of hydrogen peroxide and chloride ion. Chlorides 92-100 myeloperoxidase Homo sapiens 35-50 24915973-15 2014 Hence, the microparticle-associated myeloperoxidase-hydrogen peroxide-chloride system may contribute to widespread endothelial cell damage in conditions of neutrophil activation as observed in vasculitis and sepsis. Chlorides 70-78 myeloperoxidase Homo sapiens 36-51 22982051-1 2012 2-Chlorohexadecanal (2-ClHDA), a chlorinated fatty aldehyde, is formed via attack on ether-phospholipids by hypochlorous acid (HOCl) that is generated by the myeloperoxidase-hydrogen peroxide-chloride system of activated leukocytes. Chlorides 192-200 myeloperoxidase Homo sapiens 158-173 23306200-11 2013 In the presence of chloride and hydrogen peroxide, ceruloplasmin converted myeloperoxidase to Compound II and slowed its conversion back to the ferric enzyme. Chlorides 19-27 myeloperoxidase Homo sapiens 75-90 22881869-6 2013 MPO has many substrates, but its main phagosomal reactions should be to dismutate superoxide and, provided adequate chloride, catalyze efficient conversion of hydrogen peroxide to hypochlorous acid (HOCl). Chlorides 116-124 myeloperoxidase Homo sapiens 0-3 23102772-4 2013 Here, we investigate the oxidation of N-hydroxy-l-arginine (NOHA) by hypochlorous acid (HOCl), which is generated in vivo from hydrogen peroxide and chloride by the heme enzyme, myeloperoxidase. Chlorides 149-157 myeloperoxidase Homo sapiens 178-193 23624305-1 2013 Myeloperoxidase (MPO) is a heme-containing enzyme that generates hypochlorous acid (HOCl) from chloride (Cl(-)) and hydrogen peroxide (H2O2). Chlorides 95-103 myeloperoxidase Homo sapiens 0-15 23624305-1 2013 Myeloperoxidase (MPO) is a heme-containing enzyme that generates hypochlorous acid (HOCl) from chloride (Cl(-)) and hydrogen peroxide (H2O2). Chlorides 95-103 myeloperoxidase Homo sapiens 17-20 23626907-5 2013 In this work, we tried to explain enzymatic oxidation in terms of redox potentials by employing competitive substrates for MPO such as chloride, which is oxidized by MPO to form a strong oxidant (hypochlorite), and antioxidants that have lower redox potentials than CNTs. Chlorides 135-143 myeloperoxidase Homo sapiens 123-126 23626907-5 2013 In this work, we tried to explain enzymatic oxidation in terms of redox potentials by employing competitive substrates for MPO such as chloride, which is oxidized by MPO to form a strong oxidant (hypochlorite), and antioxidants that have lower redox potentials than CNTs. Chlorides 135-143 myeloperoxidase Homo sapiens 166-169 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. Chlorides 49-57 myeloperoxidase Homo sapiens 35-38 22902565-1 2012 Optimal and efficient killing of ingested microbes by human neutrophils is mediated in large part by the action of hypochlorous acid produced by the myeloperoxidase-H(2)O(2)-chloride system in phagosomes. Chlorides 174-182 myeloperoxidase Homo sapiens 149-164 22462755-3 2012 HOCl is generated by myeloperoxidase, (MPO) using chloride and hydrogen peroxide as substrates. Chlorides 50-58 myeloperoxidase Homo sapiens 21-36 22462755-3 2012 HOCl is generated by myeloperoxidase, (MPO) using chloride and hydrogen peroxide as substrates. Chlorides 50-58 myeloperoxidase Homo sapiens 39-42 21854003-1 2011 Myeloperoxidase (MPO) is the most abundant neutrophil enzyme and catalyzes predominantly the two-electron oxidation of ubiquitous chloride to generate the potent bleaching hypochlorous acid, thus contributing to pathogen killing as well as inflammatory diseases. Chlorides 130-138 myeloperoxidase Homo sapiens 0-15 22355012-2 2012 Whereas all MHPs oxidize specific halides to generate the corresponding hypohalous acid, MPO is unique in its capacity to oxidize chloride at physiologic pH to produce hypochlorous acid (HOCl), a potent microbicide that contributes to neutrophil-mediated host defense against infection. Chlorides 130-138 myeloperoxidase Homo sapiens 89-92 22526679-2 2012 Myeloperoxidase (MPO) is expressed in phagocytes and is the only animal heme peroxidase previously reported to be capable of using chloride ion as a substrate to form the highly microbicidal species hypochlorous acid (HOCl) at neutral pH. Chlorides 131-139 myeloperoxidase Homo sapiens 0-15 22526679-2 2012 Myeloperoxidase (MPO) is expressed in phagocytes and is the only animal heme peroxidase previously reported to be capable of using chloride ion as a substrate to form the highly microbicidal species hypochlorous acid (HOCl) at neutral pH. Chlorides 131-139 myeloperoxidase Homo sapiens 17-20 22526679-8 2012 Like MPO, VPO1 in the presence of H2O2 and chloride generates HOCl. Chlorides 43-51 myeloperoxidase Homo sapiens 5-8 22718769-9 2012 Here the dye well reflected the different substrate specificities of myeloperoxidase and eosinophil peroxidase regarding chloride and bromide. Chlorides 121-129 myeloperoxidase Homo sapiens 69-84 22002086-3 2011 The model consists of all known reactions and rate constants for reactions of superoxide, hydrogen peroxide, and chloride ions with MPO, except for the reaction of superoxide with compound I, which could only be estimated. Chlorides 113-121 myeloperoxidase Homo sapiens 132-135 22002086-4 2011 Compound I is a transitory redox intermediate of MPO that is responsible for oxidizing chloride ions to hypochlorous acid. Chlorides 87-95 myeloperoxidase Homo sapiens 49-52 21854003-1 2011 Myeloperoxidase (MPO) is the most abundant neutrophil enzyme and catalyzes predominantly the two-electron oxidation of ubiquitous chloride to generate the potent bleaching hypochlorous acid, thus contributing to pathogen killing as well as inflammatory diseases. Chlorides 130-138 myeloperoxidase Homo sapiens 17-20 21266577-5 2011 Urate competed with chloride for oxidation by MPO and at hyperuricemic levels is expected to be a substantive substrate for the enzyme. Chlorides 20-28 myeloperoxidase Homo sapiens 46-49 21708126-2 2011 The potent oxidant hypochlorous acid (HOCl), generated by the myeloperoxidase-H(2)O(2)-chloride system of activated phagocytes, converts low-density lipoprotein (LDL) into a proinflammatory lipoprotein particle. Chlorides 87-95 myeloperoxidase Homo sapiens 62-77 21708126-9 2011 We provide convincing evidence that formation of HOCl-modified (lipo)proteins generated by the myeloperoxidase-H(2)O(2)-chloride system contributes to apoptosis in T-cells. Chlorides 120-128 myeloperoxidase Homo sapiens 95-110 19622015-2 2009 Enzymatically active MPO, together with hydrogen peroxide and chloride, produces the powerful oxidant hypochlorous acid and is a key contributor to the oxygen-dependent microbicidal activity of phagocytes. Chlorides 62-70 myeloperoxidase Homo sapiens 21-24 21194373-3 2011 One of the predominant oxidants at these places is hypochlorous acid which is formed from hydrogen peroxide and chloride ions by neutrophil myeloperoxidase. Chlorides 112-120 myeloperoxidase Homo sapiens 140-155 20870018-2 2010 This reaction, catalyzed by myeloperoxidase, requires chloride anion (Cl(-)) as a substrate. Chlorides 54-68 myeloperoxidase Homo sapiens 28-43 20545824-3 2010 Melatonin also inhibits myeloperoxidase, the enzyme that catalyzes the oxidation of chloride to HOCl. Chlorides 84-92 myeloperoxidase Homo sapiens 24-39 21194373-4 2011 In this study, inactivation of human kininogens after oxidation with the myeloperoxidase-H2O2-chloride system was observed and analyzed by protein chemistry methods. Chlorides 94-102 myeloperoxidase Homo sapiens 73-88 21857088-1 2011 Myeloperoxidase (MPO) is an important enzyme that catalyzes the reaction between hydrogen peroxide and chloride to generate hypochlorous acid, which oxidizes a range of biomolecules and has been associated with inflammatory diseases. Chlorides 103-111 myeloperoxidase Homo sapiens 0-15 21857088-1 2011 Myeloperoxidase (MPO) is an important enzyme that catalyzes the reaction between hydrogen peroxide and chloride to generate hypochlorous acid, which oxidizes a range of biomolecules and has been associated with inflammatory diseases. Chlorides 103-111 myeloperoxidase Homo sapiens 17-20 20525179-1 2010 BACKGROUND: Myeloperoxidase (MPO), an important element of the microbicidal activity of neutrophils, generates hypochlorous acid (HOCl) from H2O2 and chloride, which is released into body fluids. Chlorides 150-158 myeloperoxidase Homo sapiens 12-27 20525179-1 2010 BACKGROUND: Myeloperoxidase (MPO), an important element of the microbicidal activity of neutrophils, generates hypochlorous acid (HOCl) from H2O2 and chloride, which is released into body fluids. Chlorides 150-158 myeloperoxidase Homo sapiens 29-32 20089668-1 2010 Chloride serves as a critical component of innate host defense against infection, providing the substrate for MPO-catalyzed production of HOCl in the phagosome of human neutrophils. Chlorides 0-8 myeloperoxidase Homo sapiens 110-113 19812385-3 2010 HOCl is produced from hydrogen peroxide and chloride ions through the action of myeloperoxidase. Chlorides 44-52 myeloperoxidase Homo sapiens 80-95 19800968-1 2010 Myeloperoxidase catalyzes the reaction of chloride ions with H(2)O(2) to yield hypochlorous acid (HOCl), which can damage proteins. Chlorides 42-50 myeloperoxidase Homo sapiens 0-15 19828014-4 2009 In the present study, we show that serotonin is a favoured substrate for myeloperoxidase because other physiological substrates for this enzyme, including chloride, did not affect its rate of oxidation. Chlorides 155-163 myeloperoxidase Homo sapiens 73-88 19775156-13 2009 Purified myeloperoxidase used hydrogen peroxide and chloride to catalyze the oxidation of N-terminal methionines to dehydromethionine. Chlorides 52-60 myeloperoxidase Homo sapiens 9-24 19608745-6 2009 It completely lost its ability to oxidize chloride to hypochlorous acid, which is a characteristic feature of MPO and essential for its role in host defense. Chlorides 42-50 myeloperoxidase Homo sapiens 110-113 19577554-2 2009 As detected by MALDI-TOF mass spectrometry hypochlorous acid and the myeloperoxidase-hydrogen peroxide-chloride system convert 1,2-dipalmitoyl-sn-glycero-3-phosphoserine into 1,2-dipalmitoyl-sn-glycero-3-phosphoacetaldehyde and 1,2-dipalmitoyl-sn-glycero-3-phosphonitrile. Chlorides 103-111 myeloperoxidase Homo sapiens 69-84 19464362-0 2009 Myeloperoxidase interaction with peroxynitrite: chloride deficiency and heme depletion. Chlorides 48-56 myeloperoxidase Homo sapiens 0-15 19464362-1 2009 Myeloperoxidase (MPO) is a hemoprotein involved in the leukocyte-mediated defense mechanism and uses hydrogen peroxide (H2O2) and chloride (Cl(-)) to produce hypochlorous acid. Chlorides 130-138 myeloperoxidase Homo sapiens 0-15 19464362-1 2009 Myeloperoxidase (MPO) is a hemoprotein involved in the leukocyte-mediated defense mechanism and uses hydrogen peroxide (H2O2) and chloride (Cl(-)) to produce hypochlorous acid. Chlorides 130-138 myeloperoxidase Homo sapiens 17-20 19464362-9 2009 Chloride binding to the active site of MPO constrains ONOO(-) binding by filling the space directly above the heme moiety or by causing a protein conformational change that constricts the distal heme pocket, thus preventing ONOO(-) from binding to MPO heme iron. Chlorides 0-8 myeloperoxidase Homo sapiens 39-42 19464362-9 2009 Chloride binding to the active site of MPO constrains ONOO(-) binding by filling the space directly above the heme moiety or by causing a protein conformational change that constricts the distal heme pocket, thus preventing ONOO(-) from binding to MPO heme iron. Chlorides 0-8 myeloperoxidase Homo sapiens 248-251 19464255-2 2009 Hypochlorous acid (HOCl), a potent two-electron oxidant formed by the MPO-H(2)O(2)-chloride system of activated phagocytes, modifies antiatherogenic high-density lipoprotein (HDL). Chlorides 83-91 myeloperoxidase Homo sapiens 70-73 19345674-0 2009 Formation of cholesterol ozonolysis products through an ozone-free mechanism mediated by the myeloperoxidase-H2O2-chloride system. Chlorides 114-122 myeloperoxidase Homo sapiens 93-108 19379130-1 2009 Tissue damage resulting from the extracellular production of HOCl (hypochlorous acid) by the MPO (myeloperoxidase)-hydrogen peroxide-chloride system of activated phagocytes is implicated as a key event in the progression of a number of human inflammatory diseases. Chlorides 133-141 myeloperoxidase Homo sapiens 93-96 19379130-1 2009 Tissue damage resulting from the extracellular production of HOCl (hypochlorous acid) by the MPO (myeloperoxidase)-hydrogen peroxide-chloride system of activated phagocytes is implicated as a key event in the progression of a number of human inflammatory diseases. Chlorides 133-141 myeloperoxidase Homo sapiens 98-113 18698849-8 2008 A similar selectivity of reaction and extent of thiol oxidation were also observed with myeloperoxidase in the presence of hydrogen peroxide and chloride ions. Chlorides 145-153 myeloperoxidase Homo sapiens 88-103 18851713-1 2009 MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous acids. Chlorides 49-57 myeloperoxidase Homo sapiens 0-3 18851713-1 2009 MPO (myeloperoxidase) catalyses the oxidation of chloride, bromide and thiocyanate to their respective hypohalous acids. Chlorides 49-57 myeloperoxidase Homo sapiens 5-20 18279963-1 2008 Myeloperoxidase (MPO) is a dominating enzyme of circulating polymorphonuclear neutrophils that catalyzes the two-electron oxidation of chloride, thereby producing the strong halogenating agent hypochlorous acid (ClO(-)/HOCl). Chlorides 135-143 myeloperoxidase Homo sapiens 0-15 18331758-1 2008 The enzyme myeloperoxidase shows several unusual properties compared to other peroxidases, e.g. a red-shifted absorption spectrum and a peroxidase activity towards chloride. Chlorides 164-172 myeloperoxidase Homo sapiens 11-26 18296711-2 2008 Among the different lipoprotein classes, anti-atherogenic high-density lipoprotein (HDL) represents a major target for modification by hypochlorous acid (HOCl), generated from H2O2 by MPO in the presence of physiological chloride concentrations. Chlorides 221-229 myeloperoxidase Homo sapiens 184-187 18558355-2 2008 MPO produces a highly deleterious reactive oxygen species, the hypochlorous acid (HOCl), using hydrogen peroxide (H(2)O(2)) and chloride ions as substrate. Chlorides 128-136 myeloperoxidase Homo sapiens 0-3 18353929-1 2008 Chloride anion is essential for myeloperoxidase (MPO) to produce hypochlorous acid (HOCl) in polymorphonuclear neutrophils (PMNs). Chlorides 0-14 myeloperoxidase Homo sapiens 49-52 18353929-8 2008 We previously reported that neutrophils from CF patients are defective in chlorination of ingested bacteria, suggesting that the chloride channel defect might impair the MPO-hydrogen peroxide-chloride microbicidal function. Chlorides 129-137 myeloperoxidase Homo sapiens 170-173 18279680-0 2008 Potential role of tryptophan and chloride in the inhibition of human myeloperoxidase. Chlorides 33-41 myeloperoxidase Homo sapiens 69-84 18279680-1 2008 Myeloperoxidase (MPO) binds H2O2 in the absence and presence of chloride (Cl-) and catalyzes the formation of potent oxidants through 1e(-) and 2e(-) oxidation pathways. Chlorides 64-72 myeloperoxidase Homo sapiens 0-15 18279680-1 2008 Myeloperoxidase (MPO) binds H2O2 in the absence and presence of chloride (Cl-) and catalyzes the formation of potent oxidants through 1e(-) and 2e(-) oxidation pathways. Chlorides 64-72 myeloperoxidase Homo sapiens 17-20 18279963-1 2008 Myeloperoxidase (MPO) is a dominating enzyme of circulating polymorphonuclear neutrophils that catalyzes the two-electron oxidation of chloride, thereby producing the strong halogenating agent hypochlorous acid (ClO(-)/HOCl). Chlorides 135-143 myeloperoxidase Homo sapiens 17-20 17381162-3 2007 It is generally accepted that superoxide is a precursor of hydrogen peroxide which myeloperoxidase uses to oxidize chloride to hypochlorous acid. Chlorides 115-123 myeloperoxidase Homo sapiens 83-98 17604010-0 2007 Influence of chloride on modification of unsaturated phosphatidylcholines by the myeloperoxidase/hydrogen peroxide/bromide system. Chlorides 13-21 myeloperoxidase Homo sapiens 81-96 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. Chlorides 85-93 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. Chlorides 85-93 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). Chlorides 63-71 myeloperoxidase Homo sapiens 188-203 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). Chlorides 63-71 myeloperoxidase Homo sapiens 231-234 17577734-1 2007 Hypochlorite (HOCl), the product of the activated myeloperoxidase/H(2)O(2)/chloride (MPO/H(2)O(2)/Cl(- )) system is favored as a trigger of LDL modifications, which may play a pivotal role in early atherogenesis. Chlorides 75-83 myeloperoxidase Homo sapiens 50-65 17577734-1 2007 Hypochlorite (HOCl), the product of the activated myeloperoxidase/H(2)O(2)/chloride (MPO/H(2)O(2)/Cl(- )) system is favored as a trigger of LDL modifications, which may play a pivotal role in early atherogenesis. Chlorides 75-83 myeloperoxidase Homo sapiens 85-88 18237195-4 2008 In the presence of chloride (Cl-), melatonin inactivated MPO at two points in the classic peroxidase cycle through binding to MPO to form an inactive complex, melatonin-MPO-Cl, and accelerating MPO compound II formation, an inactive form of MPO. Chlorides 19-27 myeloperoxidase Homo sapiens 57-60 18237195-4 2008 In the presence of chloride (Cl-), melatonin inactivated MPO at two points in the classic peroxidase cycle through binding to MPO to form an inactive complex, melatonin-MPO-Cl, and accelerating MPO compound II formation, an inactive form of MPO. Chlorides 19-27 myeloperoxidase Homo sapiens 126-129 18237195-4 2008 In the presence of chloride (Cl-), melatonin inactivated MPO at two points in the classic peroxidase cycle through binding to MPO to form an inactive complex, melatonin-MPO-Cl, and accelerating MPO compound II formation, an inactive form of MPO. Chlorides 19-27 myeloperoxidase Homo sapiens 126-129 18237195-4 2008 In the presence of chloride (Cl-), melatonin inactivated MPO at two points in the classic peroxidase cycle through binding to MPO to form an inactive complex, melatonin-MPO-Cl, and accelerating MPO compound II formation, an inactive form of MPO. Chlorides 19-27 myeloperoxidase Homo sapiens 126-129 18237195-4 2008 In the presence of chloride (Cl-), melatonin inactivated MPO at two points in the classic peroxidase cycle through binding to MPO to form an inactive complex, melatonin-MPO-Cl, and accelerating MPO compound II formation, an inactive form of MPO. Chlorides 19-27 myeloperoxidase Homo sapiens 126-129 17726014-4 2007 Here, we show that HOCl generated by the MPO-H2O2-chloride system inactivates TIMP-1 by oxidizing its N-terminal cysteine. Chlorides 50-58 myeloperoxidase Homo sapiens 41-44 17592500-3 2007 A unique activity of MPO is its ability to use chloride as a cosubstrate with hydrogen peroxide to generate chlorinating oxidants such as hypochlorous acid, a potent antimicrobial agent. Chlorides 47-55 myeloperoxidase Homo sapiens 21-24 17868637-1 2007 Myeloperoxidase (MPO) catalyzes the two-electron oxidation of chloride, thereby producing hypochlorous acid (HOCl). Chlorides 62-70 myeloperoxidase Homo sapiens 0-15 17868637-1 2007 Myeloperoxidase (MPO) catalyzes the two-electron oxidation of chloride, thereby producing hypochlorous acid (HOCl). Chlorides 62-70 myeloperoxidase Homo sapiens 17-20 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. Chlorides 53-61 myeloperoxidase Homo sapiens 93-96 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. Chlorides 75-83 myeloperoxidase Homo sapiens 93-96 17218539-2 2007 Recent observations have shown that the myeloperoxidase-H2O2-chloride system of activated phagocytes is highly up-regulated under inflammatory conditions where hypochlorous acid (HOCl) is formed as the major oxidant. Chlorides 61-69 myeloperoxidase Homo sapiens 40-55 17218539-5 2007 We show that albumin modified with physiologically relevant concentrations of HOCl, added as reagent or generated by the myeloperoxidase-H2O2-chloride system, is a high affinity ligand for RAGE. Chlorides 142-150 myeloperoxidase Homo sapiens 121-136 17074761-2 2006 Myeloperoxidase converts chloride and hydrogen peroxide to hypochlorous acid (HOCl), which is strongly microbicidal. Chlorides 25-33 myeloperoxidase Homo sapiens 0-15 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. Chlorides 19-27 myeloperoxidase Homo sapiens 55-70 16506790-1 2006 The highly basic heme enzyme myeloperoxidase (MPO), which is released by activated phagocytes, catalyzes the production of the potent oxidant hypochlorite (HOCl) from H(2)O(2) and chloride ions (Cl(-)). Chlorides 180-188 myeloperoxidase Homo sapiens 29-44 16506790-1 2006 The highly basic heme enzyme myeloperoxidase (MPO), which is released by activated phagocytes, catalyzes the production of the potent oxidant hypochlorite (HOCl) from H(2)O(2) and chloride ions (Cl(-)). Chlorides 180-188 myeloperoxidase Homo sapiens 46-49 17042493-1 2006 Myeloperoxidase (MPO) (donor, hydrogen peroxide oxidoreductase, EC 1.11.1.7) is the most abundant neutrophil enzyme and catalyzes predominantly the two-electron oxidation of ubiquitous chloride (Cl-), to generate the potent bleaching oxidant hypochlorous acid (HOCl), thus contributing to bacterial killing and inflammatory reactions of neutrophils. Chlorides 185-193 myeloperoxidase Homo sapiens 0-15 17042493-1 2006 Myeloperoxidase (MPO) (donor, hydrogen peroxide oxidoreductase, EC 1.11.1.7) is the most abundant neutrophil enzyme and catalyzes predominantly the two-electron oxidation of ubiquitous chloride (Cl-), to generate the potent bleaching oxidant hypochlorous acid (HOCl), thus contributing to bacterial killing and inflammatory reactions of neutrophils. Chlorides 185-193 myeloperoxidase Homo sapiens 17-20 16488068-8 2006 Myeloperoxidase treatment of LDL in the presence of chloride, H(2)O(2) and tryptophan protected the lipoprotein from subsequent cell-mediated oxidation. Chlorides 52-60 myeloperoxidase Homo sapiens 0-15 16125131-15 2006 We conclude that at physiological concentrations of chloride and bromide, hypobromous acid can be a major oxidant produced by myeloperoxidase. Chlorides 52-60 myeloperoxidase Homo sapiens 126-141 16125131-0 2006 Bromination and chlorination reactions of myeloperoxidase at physiological concentrations of bromide and chloride. Chlorides 105-113 myeloperoxidase Homo sapiens 42-57 16125131-4 2006 We have investigated the ability of myeloperoxidase to produce hypobromous acid in the presence of physiological concentrations of chloride and bromide. Chlorides 131-139 myeloperoxidase Homo sapiens 36-51 16171780-0 2005 Thiol-containing molecules interact with the myeloperoxidase/H2O2/chloride system to inhibit LDL oxidation. Chlorides 66-74 myeloperoxidase Homo sapiens 45-60 16260376-1 2005 Upon inflammation, activated neutrophils secrete myeloperoxidase, an enzyme able to generate hypochlorous acid (HOCl) from hydrogen peroxide and chloride ions. Chlorides 145-153 myeloperoxidase Homo sapiens 49-64 15689384-5 2005 Among the antimicrobial systems formed in the phagosome is one consisting of myeloperoxidase (MPO), released into the phagosome during the degranulation process, hydrogen peroxide (H2O2), formed by the respiratory burst and a halide, particularly chloride. Chlorides 247-255 myeloperoxidase Homo sapiens 77-92 15913556-2 2005 It is produced from H2O2 and chloride by the heme enzyme myeloperoxidase (MPO). Chlorides 29-37 myeloperoxidase Homo sapiens 57-72 15913556-2 2005 It is produced from H2O2 and chloride by the heme enzyme myeloperoxidase (MPO). Chlorides 29-37 myeloperoxidase Homo sapiens 74-77 15882077-1 2005 Hypochlorous acid (HOCl) is a powerful oxidant generated from H(2)O(2) and chloride ions by the heme enzyme myeloperoxidase (MPO) released from activated leukocytes. Chlorides 75-83 myeloperoxidase Homo sapiens 108-123 15882077-1 2005 Hypochlorous acid (HOCl) is a powerful oxidant generated from H(2)O(2) and chloride ions by the heme enzyme myeloperoxidase (MPO) released from activated leukocytes. Chlorides 75-83 myeloperoxidase Homo sapiens 125-128 15689384-5 2005 Among the antimicrobial systems formed in the phagosome is one consisting of myeloperoxidase (MPO), released into the phagosome during the degranulation process, hydrogen peroxide (H2O2), formed by the respiratory burst and a halide, particularly chloride. Chlorides 247-255 myeloperoxidase Homo sapiens 94-97 15689384-6 2005 The initial product of the MPO-H2O2-chloride system is hypochlorous acid, and subsequent formation of chlorine, chloramines, hydroxyl radicals, singlet oxygen, and ozone has been proposed. Chlorides 36-44 myeloperoxidase Homo sapiens 27-30 15514213-2 2004 Modification of high-density lipoprotein (HDL) by hypochlorous acid/hypochlorite (HOCl/OCl-) [correction]-generated in vivo by the myeloperoxidase-hydrogen peroxide-chloride system of activated phagocytes-forms a proatherogenic lipoprotein particle that binds to and is internalized by endothelial cells. Chlorides 165-173 myeloperoxidase Homo sapiens 131-146 15514213-7 2004 CONCLUSIONS: 2-Chlorohexadecanal, produced by the myeloperoxidase-hydrogen peroxide-chloride system of activated phagocytes may act as a mediator of vascular injury associated with ischemia-reperfusion injury, glomerulosclerosis, and atherosclerosis. Chlorides 84-92 myeloperoxidase Homo sapiens 50-65 15078224-2 2004 Reaction of MPO with H2O2 in the presence of chloride ions generates HOCl (the physiological mixture of hypochlorous acid and its anion present at pH 7.4). Chlorides 45-53 myeloperoxidase Homo sapiens 12-15 15507767-1 2004 Myeloperoxidase (MPO) uses hydrogen peroxide to oxidize chloride to hypochlorous acid. Chlorides 56-64 myeloperoxidase Homo sapiens 0-15 15507767-1 2004 Myeloperoxidase (MPO) uses hydrogen peroxide to oxidize chloride to hypochlorous acid. Chlorides 56-64 myeloperoxidase Homo sapiens 17-20 15493876-2 2004 We studied MPO-mediated formation of conjugated dienes in isolated human LDL in dependence on the concentrations of nitrite and chloride. Chlorides 128-136 myeloperoxidase Homo sapiens 11-14 15203186-3 2004 Chloride is supposed to be the major substrate for MPO, generating reactive hypochlorous acid (HOCl), modifying LDL. Chlorides 0-8 myeloperoxidase Homo sapiens 51-54 14599211-1 2003 Myeloperoxidase released from activated phagocytes reacts with H(2)O(2) in the presence of chloride ions to give hypochlorous acid. Chlorides 91-99 myeloperoxidase Homo sapiens 0-15 14633118-4 2003 The ability of MPO to generate hypochlorous acid/hypochlorite (HOCl/OCl-) from hydrogen peroxide in the presence of chloride ions is a unique and defining activity for this enzyme. Chlorides 116-124 myeloperoxidase Homo sapiens 15-18 14633118-5 2003 The MPO-hydrogen peroxide-chloride system leads to a variety of chlorinated protein and lipid adducts that in turn may cause dysfunction of cells in different compartments of the kidney. Chlorides 26-34 myeloperoxidase Homo sapiens 4-7 14633118-6 2003 The aim of this article is to cover and interpret some experimental and clinical aspects in glomerular and tubulointerstitial diseases in which the MPO-hydrogen peroxide-chloride system has been considered an important pathophysiologic factor in the progression but also the attenuation of experimental renal disease. Chlorides 170-178 myeloperoxidase Homo sapiens 148-151 14633118-8 2003 Specifically, the interaction of MPO with nitric oxide metabolism adds to the complexity of actions of oxidants and may help to explain bimodal partly detrimental partly beneficial effects of the MPO-hydrogen peroxide-chloride system in redox-modulated renal diseases. Chlorides 218-226 myeloperoxidase Homo sapiens 33-36 14633118-8 2003 Specifically, the interaction of MPO with nitric oxide metabolism adds to the complexity of actions of oxidants and may help to explain bimodal partly detrimental partly beneficial effects of the MPO-hydrogen peroxide-chloride system in redox-modulated renal diseases. Chlorides 218-226 myeloperoxidase Homo sapiens 196-199 14740428-8 2003 Myeloperoxidase produces not only the strong oxidant bleach (hypochlorous acid) out of hydrogen peroxide and chloride ions but also oxidizes LDL into a macrophage high-uptake form, inactivates protease inhibitors, and consumes nitric oxide. Chlorides 109-117 myeloperoxidase Homo sapiens 0-15 12787959-2 2003 The heme enzyme MPO catalyzes the conversion of hydrogen peroxide and chloride to hypochlorous acid. Chlorides 70-78 myeloperoxidase Homo sapiens 16-19 12060654-0 2002 Human neutrophils use the myeloperoxidase-hydrogen peroxide-chloride system to chlorinate but not nitrate bacterial proteins during phagocytosis. Chlorides 60-68 myeloperoxidase Homo sapiens 26-41 12614844-1 2003 The formation of lysophosphatidylcholines and chlorohydrins from unsaturated phosphatidylcholines upon the treatment with the myeloperoxidase-hydrogen peroxide-chloride system was evaluated by means of matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. Chlorides 160-168 myeloperoxidase Homo sapiens 126-141 12606047-1 2003 In the presence of a H(2)O(2)-generating system, myeloperoxidase (MPO) caused conjugated diene formation in low-density lipoprotein (LDL), indicating lipid peroxidation which was dependent on nitrite but not on chloride. Chlorides 211-219 myeloperoxidase Homo sapiens 49-64 12606047-1 2003 In the presence of a H(2)O(2)-generating system, myeloperoxidase (MPO) caused conjugated diene formation in low-density lipoprotein (LDL), indicating lipid peroxidation which was dependent on nitrite but not on chloride. Chlorides 211-219 myeloperoxidase Homo sapiens 66-69 12505315-3 2002 Hypochlorous acid (HOCl), produced by myeloperoxidase-catalysed oxidation of chloride by hydrogen peroxide, is the major strong oxidant generated by these cells. Chlorides 77-85 myeloperoxidase Homo sapiens 38-53 12060654-9 2002 Our observations support the view that the phagolysosome of human neutrophils uses the myeloperoxidase-hydrogen peroxide-chloride system to chlorinate bacterial proteins. Chlorides 121-129 myeloperoxidase Homo sapiens 87-102 11513598-1 2001 The predominant physiological activity of myeloperoxidase is to convert hydrogen peroxide and chloride to hypochlorous acid. Chlorides 94-102 myeloperoxidase Homo sapiens 42-57 11934280-4 2002 Since myeloperoxidase is the only human enzyme known to convert chloride ions into the cytotoxic hypochlorous acid, the data presented in this paper bear relevance to the pharmacological effects of aminoglycoside antibiotics, which, while inhibiting bacterial growth, also prevent oxidative cellular damage caused by hypochlorous acid aging as substrates and inhibitors of myeloperoxidase. Chlorides 64-72 myeloperoxidase Homo sapiens 6-21 11934280-4 2002 Since myeloperoxidase is the only human enzyme known to convert chloride ions into the cytotoxic hypochlorous acid, the data presented in this paper bear relevance to the pharmacological effects of aminoglycoside antibiotics, which, while inhibiting bacterial growth, also prevent oxidative cellular damage caused by hypochlorous acid aging as substrates and inhibitors of myeloperoxidase. Chlorides 64-72 myeloperoxidase Homo sapiens 373-388 11677044-8 2001 Mono-chlorohydrins of 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine were detected after the incubation of the latter phospholipid with the myeloperoxidase-hydrogen peroxide-chloride system at pH 6.0. Chlorides 175-183 myeloperoxidase Homo sapiens 141-156 11677044-10 2001 Thus, mono-chlorohydrins in 1-stearoyl-2-oleoyl-sn-glycero-3-phosphocholine produced by hypochlorous acid from the myeloperoxidase-hydrogen peroxide-chloride system can also be detected by means of MALDI-TOF MS. Chlorides 149-157 myeloperoxidase Homo sapiens 115-130 11705694-3 2001 The phagocyte-derived myeloperoxidase-hydrogen peroxide-chloride system generates hypochlorous acid, which reacts with tyrosine residues of proteins to form 3-chlorotyrosine. Chlorides 56-64 myeloperoxidase Homo sapiens 22-37 11791891-2 2001 During phagocytosis, MPO catalyzes a peroxidative reaction using chloride ion and hydrogen peroxide (H2O2) as substrate. Chlorides 65-77 myeloperoxidase Homo sapiens 21-24 11594511-2 2001 Delivered from its storage compartment to the phagolysosome during fusion of the azurophilic granules, MPO catalyzes the oxidation of chloride in the presence of H2O2, chemistry unique to MPO, and thereby generates an array of highly reactive oxidants. Chlorides 134-142 myeloperoxidase Homo sapiens 103-106 11594511-2 2001 Delivered from its storage compartment to the phagolysosome during fusion of the azurophilic granules, MPO catalyzes the oxidation of chloride in the presence of H2O2, chemistry unique to MPO, and thereby generates an array of highly reactive oxidants. Chlorides 134-142 myeloperoxidase Homo sapiens 188-191 11358505-0 2001 Purification and structure of the major product obtained by reaction of NADPH and NMNH with the myeloperoxidase/hydrogen peroxide/chloride system. Chlorides 130-138 myeloperoxidase Homo sapiens 96-111 11422382-3 2001 At plasma concentrations of halide ion, hypochlorous acid is a major product of the myeloperoxidase-hydrogen peroxide-chloride system. Chlorides 118-126 myeloperoxidase Homo sapiens 84-99 11297432-3 2001 In the current studies, we show that hypochlorous acid (HOCl), generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes, cross-links single-stranded DNA-binding protein (SSB) to single-stranded oligonucleotides. Chlorides 114-122 myeloperoxidase Homo sapiens 80-95 11304574-1 2001 Myeloperoxidase (MPO), which is released from cytoplasmic granules of activated phagocytes by a degranulation process, reacts with H(2)O(2) (generated during the oxidative burst) and chloride ions to generate hypochlorous acid/hypochlorite (HOCl/OCl(-)). Chlorides 183-191 myeloperoxidase Homo sapiens 0-15 11304574-1 2001 Myeloperoxidase (MPO), which is released from cytoplasmic granules of activated phagocytes by a degranulation process, reacts with H(2)O(2) (generated during the oxidative burst) and chloride ions to generate hypochlorous acid/hypochlorite (HOCl/OCl(-)). Chlorides 183-191 myeloperoxidase Homo sapiens 17-20 11304574-8 2001 HOCl-modified proteins, products of the MPO-H(2)O(2)-chloride system in vivo, were not present intracellularly, but immunoreactivity for HOCl-modified proteins was cell-associated and/or present in the extracellular matrix. Chlorides 53-61 myeloperoxidase Homo sapiens 40-43 11297432-7 2001 The covalent complex of radiolabeled dT(40) and SSB was also generated by chloramines and the complete myeloperoxidase-hydrogen peroxide-chloride system. Chlorides 137-145 myeloperoxidase Homo sapiens 103-118 11297432-8 2001 The enzymatic reaction required each component of the system and was inhibited by heme poisons and chloride-free conditions, implicating myeloperoxidase and HOCl. Chlorides 99-107 myeloperoxidase Homo sapiens 137-152 10814547-6 2000 Purified recombinant human LPO and MPO, both with a molecular mass of about 80 kDa, showed properties similar to bovine LPO and human MPO, respectively, in terms of absorption spectrum, sensitivity to dapsone, specificity for chloride ions, and reactivity with anti-bovine LPO or anti-MPO antibodies. Chlorides 226-234 myeloperoxidase Homo sapiens 35-38 11054430-3 2001 Furthermore, hypochlorous acid (HOCl), the major strong oxidant generated by MPO in the presence of physiological concentrations of chloride ions, can also react with nitrite, forming the reactive intermediate nitryl chloride. Chlorides 132-140 myeloperoxidase Homo sapiens 77-80 11020661-2 2000 The heme enzyme myeloperoxidase catalyzes the production of hypochlorous acid from hydrogen peroxide and chloride. Chlorides 105-113 myeloperoxidase Homo sapiens 16-31 11440179-0 2001 Chlorination of N-acetyltyrosine with HOCl, chloramines, and myeloperoxidase-hydrogen peroxide-chloride system. Chlorides 95-103 myeloperoxidase Homo sapiens 61-76 10998045-0 2000 Mechanism of reaction of myeloperoxidase with hydrogen peroxide and chloride ion. Chlorides 68-80 myeloperoxidase Homo sapiens 25-40 10998045-1 2000 The reaction of myeloperoxidase compound I (MPO-I) with chloride ion is widely assumed to produce the bacterial killing agent after phagocytosis. Chlorides 56-64 myeloperoxidase Homo sapiens 16-31 10998045-1 2000 The reaction of myeloperoxidase compound I (MPO-I) with chloride ion is widely assumed to produce the bacterial killing agent after phagocytosis. Chlorides 56-64 myeloperoxidase Homo sapiens 44-47 10998045-8 2000 It was found that the rate constant for the reaction of compound I, generated from myeloperoxidase (MPO) and excess hydrogen peroxide with chloride, decreased with increasing chloride concentration. Chlorides 139-147 myeloperoxidase Homo sapiens 83-98 10998045-8 2000 It was found that the rate constant for the reaction of compound I, generated from myeloperoxidase (MPO) and excess hydrogen peroxide with chloride, decreased with increasing chloride concentration. Chlorides 139-147 myeloperoxidase Homo sapiens 100-103 10998045-8 2000 It was found that the rate constant for the reaction of compound I, generated from myeloperoxidase (MPO) and excess hydrogen peroxide with chloride, decreased with increasing chloride concentration. Chlorides 175-183 myeloperoxidase Homo sapiens 83-98 10998045-8 2000 It was found that the rate constant for the reaction of compound I, generated from myeloperoxidase (MPO) and excess hydrogen peroxide with chloride, decreased with increasing chloride concentration. Chlorides 175-183 myeloperoxidase Homo sapiens 100-103 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. Chlorides 130-138 myeloperoxidase Homo sapiens 50-65 10766781-2 2000 Myeloperoxidase is a heme enzyme of neutrophils that uses hydrogen peroxide to oxidize chloride to hypochlorous acid. Chlorides 87-95 myeloperoxidase Homo sapiens 0-15 10766781-7 2000 In the presence of physiological concentrations of nitrite and chloride, myeloperoxidase catalyzed little nitration of tyrosyl residues in a heptapeptide. Chlorides 63-71 myeloperoxidase Homo sapiens 73-88 10608505-3 2000 We also review the enzymology that points to myeloperoxidase having a number of physiologic substrates in addition to chloride and the evidence that it produces hypochlorous acid in the neutrophil phagosome in sufficient quantities to be bactericidal. Chlorides 118-126 myeloperoxidase Homo sapiens 45-60 10805914-0 2000 Effects of pH and chloride concentration on resonance Raman spectra of human myeloperoxidase and Raman microspectroscopic analysis of enzyme state in azurophilic granules. Chlorides 18-26 myeloperoxidase Homo sapiens 77-92 10744670-4 2000 We previously showed that p-hydroxyphenylacetaldehyde (pHA) is the major product of L-tyrosine oxidation by the myeloperoxidase/hydrogen peroxide/chloride system of phagocytes. Chlorides 146-154 myeloperoxidase Homo sapiens 112-127 11996112-3 2000 In this paper the reactions of lipids (preferentially unsaturated fatty acids and cholesterol) with either reagent HOCl or HOCl generated by the MPO-hydrogen peroxide-chloride system are reviewed. Chlorides 167-175 myeloperoxidase Homo sapiens 145-148 10984130-1 2000 The phagocyte-derived enzyme myeloperoxidase has been recently implicated in the pathogenesis of atherosclerosis, because it catalyzes the reaction of hydrogen peroxide with chloride ions to give the highly toxic oxidant hypochlorous acid. Chlorides 174-182 myeloperoxidase Homo sapiens 29-44 10994869-11 2000 Among the heme peroxidases, only chloroperoxidase (for example from Caldariomyces fumago) and mammalian myeloperoxidase are able to oxidize chloride ion. Chlorides 140-148 myeloperoxidase Homo sapiens 104-119 10994869-18 2000 Also a recent clarification of the mechanism of reaction of myeloperoxidase with hydrogen peroxide and chloride along with accurate determination of the elementary rate constants will be discussed. Chlorides 103-111 myeloperoxidase Homo sapiens 60-75 10631599-1 1999 The heme group of myeloperoxidase shows anomalous optical properties, and the enzyme possesses the unique ability to catalyze the oxidation of chloride. Chlorides 143-151 myeloperoxidase Homo sapiens 18-33 10559226-0 1999 Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes produces 5-chlorocytosine in bacterial RNA. Chlorides 70-78 myeloperoxidase Homo sapiens 36-51 9895241-2 1999 Apart from this role of being a substrate for the MPO-reaction the chloride anion has been considered as unreactive and has not been implicated in radical reactions which contribute to the killing process. Chlorides 67-81 myeloperoxidase Homo sapiens 50-53 10482305-4 1999 In light of the important role of the MPO-H2O2-chloride system in human host defense, the relatively high prevalence of inherited MPO deficiency was an unanticipated insight provided by the widespread use of automated flow cytometry for the enumeration of leukocytes in clinical specimens. Chlorides 47-55 myeloperoxidase Homo sapiens 38-41 10519157-4 1999 These products of the MPO-H2O2-chloride system are powerful oxidants that can have profound biological effects. Chlorides 31-39 myeloperoxidase Homo sapiens 22-25 10519157-8 1999 MPO and H2O2 also can be released to the outside of the cell where a reaction with chloride can induce damage to adjacent tissue and, thus, contribute to the pathogenesis of disease. Chlorides 83-91 myeloperoxidase Homo sapiens 0-3 10393704-4 1999 Conversion of alpha-amino acids to aldehydes requires hypochlorous acid (HOCl), formed from H2O2 and chloride by myeloperoxidase. Chlorides 101-109 myeloperoxidase Homo sapiens 113-128 10393704-7 1999 Furthermore, Nepsilon-(carboxymethyl)lysine (CML), a chemically well-characterized AGE product, was generated on RNase A when it was exposed to reagent HOCl-serine, the myeloperoxidase-H2O2-chloride system plus L-serine, or activated human neutrophils plus L-serine. Chlorides 190-198 myeloperoxidase Homo sapiens 169-184 9989595-0 1999 Physiological production of singlet molecular oxygen in the myeloperoxidase-H2O2-chloride system. Chlorides 81-89 myeloperoxidase Homo sapiens 60-75 10593608-5 1999 At neutral pH, the rate constant for myeloperoxidase compound I reacting with serotonin is an order of magnitude larger than for its reaction with chloride, (2.2 +/- 0.2) x 10(6) M(-1) x s(-1). Chlorides 147-155 myeloperoxidase Homo sapiens 37-52 10593608-6 1999 A direct competition of serotonin with chloride for myeloperoxidase compound I oxidation was observed. Chlorides 39-47 myeloperoxidase Homo sapiens 52-67 9894014-2 1999 Our previous studies indicated that p-hydroxyphenylacetaldehyde (pHA), the major product of L-tyrosine oxidation by the myeloperoxidase/hydrogen peroxide/chloride system of phagocytes, covalently modifies the epsilon-amino group of lysine residues at sites of inflammation. Chlorides 154-162 myeloperoxidase Homo sapiens 120-135 10784377-3 1999 The aim of this study was to investigate whether the kinetics of low-density lipoprotein modification by the myeloperoxidase/hydrogen peroxide/chloride system in vitro conform to the established kinetics of hypochlorous acid formation and to compare the results with known in vivo data. Chlorides 143-151 myeloperoxidase Homo sapiens 109-124 10784377-9 1999 In summary, low-density lipoprotein modification is affected by the myeloperoxidase/hydrogen peroxide/chloride system in a similar manner to hypochlorous acid production. Chlorides 102-110 myeloperoxidase Homo sapiens 68-83 9922160-0 1998 Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate. Chlorides 44-52 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. Chlorides 246-254 myeloperoxidase Homo sapiens 58-73 9742209-8 1998 Chloride ion effects on the MPO-catalysed oxygenation of sulphides were also studied. Chlorides 0-8 myeloperoxidase Homo sapiens 28-31 9742209-9 1998 Chloride acted as a substrate for MPO and as an activator in MPO-catalysed sulphoxidation. Chlorides 0-8 myeloperoxidase Homo sapiens 34-37 9742209-9 1998 Chloride acted as a substrate for MPO and as an activator in MPO-catalysed sulphoxidation. Chlorides 0-8 myeloperoxidase Homo sapiens 61-64 9742209-11 1998 In the presence of 100 mM chloride the catalytic efficiency (kcat/Km) of MPO increased 3-4-fold, whatever the sulphide considered, but racemic products were obtained. Chlorides 26-34 myeloperoxidase Homo sapiens 73-76 9478947-0 1998 Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Chlorides 63-71 myeloperoxidase Homo sapiens 29-44 9689943-0 1998 A kinetic model of the myeloperoxidase-hydrogen peroxide-chloride ion system in phagolysosomes. Chlorides 57-65 myeloperoxidase Homo sapiens 23-38 9689943-1 1998 A kinetic model has been constructed of the myeloperoxidase-hydrogen peroxide-chloride ion system of mammalian neutrophils. Chlorides 78-86 myeloperoxidase Homo sapiens 44-59 9618427-5 1998 In the presence of hydrogen peroxide and chloride, neutrophil myeloperoxidase, an enzyme from the same gene superfamily as thyroid peroxidase, generates hypochlorous acid which inactivates alpha-1-proteinase inhibitor (A1PI) present in serum. Chlorides 41-49 myeloperoxidase Homo sapiens 62-77 9359420-0 1997 Thiocyanate and chloride as competing substrates for myeloperoxidase. Chlorides 16-24 myeloperoxidase Homo sapiens 53-68 9359420-7 1997 In the presence of 100 mM chloride, myeloperoxidase catalysed the production of hypothiocyanite at concentrations of thiocyanate as low as 25 microM. Chlorides 26-34 myeloperoxidase Homo sapiens 36-51 9359420-9 1997 The rate of H2O2 loss catalysed by myeloperoxidase in the presence of 100 mM chloride doubled when 100 microM thiocyanate was added, and was maximal with 1mM thiocyanate. Chlorides 77-85 myeloperoxidase Homo sapiens 35-50 9359420-10 1997 This indicates that at plasma concentrations of thiocyanate and chloride, myeloperoxidase is far from saturated. Chlorides 64-72 myeloperoxidase Homo sapiens 74-89 9359420-1 1997 The neutrophil enzyme myeloperoxidase uses H2O2 to oxidize chloride, bromide, iodide and thiocyanate to their respective hypohalous acids. Chlorides 59-67 myeloperoxidase Homo sapiens 22-37 9359420-4 1997 Our aim was to establish whether myeloperoxidase oxidizes thiocyanate in the presence of chloride at physiological concentrations of these substrates. Chlorides 89-97 myeloperoxidase Homo sapiens 33-48 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. Chlorides 39-47 myeloperoxidase Homo sapiens 171-186 9326240-1 1997 Myeloperoxidase (MPO) catalyzes a reaction between chloride and hydrogen peroxide to generate hypochlorous acid and other reactive compounds that have been linked to DNA damage. Chlorides 51-59 myeloperoxidase Homo sapiens 0-15 9326240-1 1997 Myeloperoxidase (MPO) catalyzes a reaction between chloride and hydrogen peroxide to generate hypochlorous acid and other reactive compounds that have been linked to DNA damage. Chlorides 51-59 myeloperoxidase Homo sapiens 17-20 9128147-2 1997 While MPO shows significant sequence homology with other peroxidases and this homology is particularly striking among the active-site residues, MPO exhibits unusual spectral features and the unique ability to catalyze the oxidation of chloride ions. Chlorides 235-243 myeloperoxidase Homo sapiens 6-9 9202012-0 1997 p-Hydroxyphenylacetaldehyde, the major product of L-tyrosine oxidation by the myeloperoxidase-H2O2-chloride system of phagocytes, covalently modifies epsilon-amino groups of protein lysine residues. Chlorides 99-107 myeloperoxidase Homo sapiens 78-93 9128147-10 1997 This change suggests that loss of the distal ligand in MPO releases stress on the heme which may facilitate binding of chloride ion. Chlorides 119-127 myeloperoxidase Homo sapiens 55-58 9128147-2 1997 While MPO shows significant sequence homology with other peroxidases and this homology is particularly striking among the active-site residues, MPO exhibits unusual spectral features and the unique ability to catalyze the oxidation of chloride ions. Chlorides 235-243 myeloperoxidase Homo sapiens 144-147 9065416-5 1997 Phenolic nitration by MPO-catalyzed NO2- oxidation is only partially inhibited by chloride (Cl-), the presumed major physiological substrate for MPO. Chlorides 82-90 myeloperoxidase Homo sapiens 22-25 9065416-5 1997 Phenolic nitration by MPO-catalyzed NO2- oxidation is only partially inhibited by chloride (Cl-), the presumed major physiological substrate for MPO. Chlorides 82-90 myeloperoxidase Homo sapiens 145-148 8567631-1 1996 A chloride-dependent mechanism for the conversion of free amino acids into reactive aldehydes by myeloperoxidase. Chlorides 2-10 myeloperoxidase Homo sapiens 97-112 9022075-0 1997 Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to convert hydroxy-amino acids into glycolaldehyde, 2-hydroxypropanal, and acrolein. Chlorides 63-71 myeloperoxidase Homo sapiens 29-44 9022075-4 1997 We now demonstrate that human neutrophils employ the myeloperoxidase-H202-chloride system to produce alpha-hydroxy and alpha,beta-unsaturated aldehydes from hydroxy-amino acids in high yield. Chlorides 74-82 myeloperoxidase Homo sapiens 53-68 9022075-9 1997 Aldehyde production by purified myeloperoxidase required H202 and chloride, and was mimicked by reagent hypochlorous acid (HOCl) in the absence of enzyme, suggesting that the reaction pathway involves a chlorinated intermediate. Chlorides 66-74 myeloperoxidase Homo sapiens 32-47 9022075-10 1997 Collectively, these results indicate that the myeloperoxidase-H202-chloride system of phagocytes converts free hydroxy-amino acids into highly reactive alpha-hydroxy and alpha,beta-unsaturated aldehydes. Chlorides 67-75 myeloperoxidase Homo sapiens 46-61 9020887-2 1997 The haem enzyme myeloperoxidase catalyses its production from hydrogen peroxide and chloride. Chlorides 84-92 myeloperoxidase Homo sapiens 16-31 8823292-2 1996 One important pathway involves the generation of potent halogenating agents by the myeloperoxidase-hydrogen peroxide-chloride system. Chlorides 117-125 myeloperoxidase Homo sapiens 83-98 8823292-5 1996 In this study gas chromatography-mass spectrometric analysis of head space gas revealed that the complete myeloperoxidase-hydrogen peroxide-chloride system generated Cl2. Chlorides 140-148 myeloperoxidase Homo sapiens 106-121 8798498-0 1996 Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols. Chlorides 70-78 myeloperoxidase Homo sapiens 36-51 8567631-4 1996 We now report that activated neutrophils utilize the myeloperoxidase-H2O2-chloride system to convert L-tyrosine to p-hydroxyphenylacetaldehyde. Chlorides 74-82 myeloperoxidase Homo sapiens 53-68 8567631-9 1996 Collectively, these results indicate that activated phagocytes, under physiological conditions, utilize myeloperoxidase to execute the chloride-dependent conversion of L-tyrosine to the lipid-soluble aldehyde, p-hydroxyphenylacetaldehyde, in near quantitative yield. Chlorides 135-143 myeloperoxidase Homo sapiens 104-119 8060981-7 1994 Three major classes of sterol oxidation products were apparent when cholesterol-phosphatidylcholine multilamellar vesicles which had been exposed to a myeloperoxidase-hydrogen peroxide-chloride system were subsequently analyzed by normal-phase thin layer chromatography. Chlorides 185-193 myeloperoxidase Homo sapiens 151-166 7622459-2 1995 It is produced from hydrogen peroxide and chloride by the heme enzyme myeloperoxidase. Chlorides 42-50 myeloperoxidase Homo sapiens 70-85 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. Chlorides 67-75 myeloperoxidase Homo sapiens 85-100 7772042-1 1995 Myeloperoxidase is the most abundant protein in neutrophils and catalyses the conversion of H2O2 and chloride into HOCl. Chlorides 101-109 myeloperoxidase Homo sapiens 0-15 18475677-1 1995 We investigated the effects of the antibiotic ceftazidime (CAZ) on the cytolytic action of the neutrophil myeloperoxidase-hydrogen peroxide-chloride anion system (MPO/H(2)O(2)/Cl(-)). Chlorides 140-148 myeloperoxidase Homo sapiens 106-121 18475677-1 1995 We investigated the effects of the antibiotic ceftazidime (CAZ) on the cytolytic action of the neutrophil myeloperoxidase-hydrogen peroxide-chloride anion system (MPO/H(2)O(2)/Cl(-)). Chlorides 140-148 myeloperoxidase Homo sapiens 163-166 8068018-3 1994 We have studied the oxidative modification of LDL by hypochlorite (-OCl), a powerful oxidant produced from H2O2 and chloride via the action of myeloperoxidase which is released from activated neutrophils and monocytes. Chlorides 116-124 myeloperoxidase Homo sapiens 143-158 8008434-10 1994 The effect of aerobic conditions on the release of elastase and the inactivation of myeloperoxidase could be ascribed to oxidants formed in the myeloperoxidase-H2O2-chloride system. Chlorides 165-173 myeloperoxidase Homo sapiens 84-99 8008434-10 1994 The effect of aerobic conditions on the release of elastase and the inactivation of myeloperoxidase could be ascribed to oxidants formed in the myeloperoxidase-H2O2-chloride system. Chlorides 165-173 myeloperoxidase Homo sapiens 144-159 8008434-11 1994 Also, the activity of the released cytoplasmic enzyme lactate dehydrogenase was inactivated by oxidants formed in the myeloperoxidase-H2O2-chloride system. Chlorides 139-147 myeloperoxidase Homo sapiens 118-133 8008434-13 1994 In this environment, the released products may also escape inactivation by the myeloperoxidase-H2O2-chloride system. Chlorides 100-108 myeloperoxidase Homo sapiens 79-94 8315349-8 1993 to H2O2, can increase the activity of the MPO-H2O2-chloride antimicrobial system released by stimulated PMNs. Chlorides 51-59 myeloperoxidase Homo sapiens 42-45 8390258-1 1993 Myeloperoxidase, the most abundant enzyme in neutrophils, catalyses the conversion of hydrogen peroxide and chloride to hypochlorous acid. Chlorides 108-116 myeloperoxidase Homo sapiens 0-15 8387748-7 1993 The reaction with myeloperoxidase required chloride and was inhibited by catalase and methionine, indicating the involvement of hypochlorite. Chlorides 43-51 myeloperoxidase Homo sapiens 18-33 1328183-6 1992 In the second mechanism, however, chloride ion is oxidized by myeloperoxidase to HOCl which reacts with 1,3-butadiene to yield CHB. Chlorides 34-42 myeloperoxidase Homo sapiens 62-77 1324677-5 1992 Dapsone was much more effective as an inhibitor of both MPO and EPO when chloride rather than tetramethylbenzidine was the substrate. Chlorides 73-81 myeloperoxidase Homo sapiens 56-59 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Chlorides 65-73 myeloperoxidase Homo sapiens 38-53 1321589-1 1992 Stimulated neutrophils produce hypochlorous acid (HOCl) via the myeloperoxidase-catalyzed reaction of hydrogen peroxide with chloride. Chlorides 125-133 myeloperoxidase Homo sapiens 64-79 1411581-3 1992 MMP-8 is activated by hypochlorous acid produced by myeloperoxidase from hydrogen peroxide and chloride ion and by the hydroxyl radical produced in Haber Weiss reaction fed by superoxide produced by, eg, NADPH (reduced nicotinamide adenine dinucleotide) oxidase and xanthine oxidase. Chlorides 95-103 myeloperoxidase Homo sapiens 52-67 1318327-7 1992 The data suggest that when PMN are stimulated, MPO released by degranulation reacts with H2O2 formed by the respiratory burst to oxidize chloride to a product (presumably hypochlorous acid) that is toxic to HIV-1. Chlorides 137-145 myeloperoxidase Homo sapiens 47-50 1656885-8 1991 Like mature MPO, recMPO has a peroxidatic activity and catalyzes the oxidation of chloride ions in the presence of hydrogen peroxide, producing hypochlorous acid as measured by the monochlorodimedon assay. Chlorides 82-90 myeloperoxidase Homo sapiens 12-15 1321719-9 1992 Chloride, which is a substrate of the enzyme not only protects myeloperoxidase against bleaching by hypochlorous acid but also competitively inhibits the binding of hypochlorous acid to myeloperoxidase, a process which also has been observed in the reaction with hydrogen peroxide. Chlorides 0-8 myeloperoxidase Homo sapiens 63-78 1321719-9 1992 Chloride, which is a substrate of the enzyme not only protects myeloperoxidase against bleaching by hypochlorous acid but also competitively inhibits the binding of hypochlorous acid to myeloperoxidase, a process which also has been observed in the reaction with hydrogen peroxide. Chlorides 0-8 myeloperoxidase Homo sapiens 186-201 1319066-2 1992 Monocytes, when stimulated, release myeloperoxidase (MPO) and produce H2O2; MPO reacts with H2O2 and chloride to form hypochlorous acid, a known microbicidal agent. Chlorides 101-109 myeloperoxidase Homo sapiens 76-79 1314821-7 1992 The addition of purified myeloperoxidase to an enzymatic superoxide generating system resulted in the detection of hydroxyl radical that was dependent upon the presence of chloride and was inhibited by superoxide dismutase, catalase, and azide. Chlorides 172-180 myeloperoxidase Homo sapiens 25-40 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Chlorides 65-73 myeloperoxidase Homo sapiens 55-58 1316115-4 1992 Degradation of MeHg and EtHg with the myeloperoxidase (MPO)-H2O2-chloride system was inhibited by MPO inhibitors (cyanide and azide), catalase, hypochlorous acid (HOCI) scavengers (glycine, alanine, serine and taurine), 1,4-diazabicyclo[2,2,2]octane and 2,5-dimethylfuran, but not by hydroxyl radical scavengers (ethanol and mannitol). Chlorides 65-73 myeloperoxidase Homo sapiens 98-101 2172341-1 1990 Neutrophil myeloperoxidase (MPO) adsorbs to bacteria as a pre-requisite for killing by the MPO/hydrogen-peroxide/chloride system. Chlorides 113-121 myeloperoxidase Homo sapiens 11-26 1650217-4 1991 Chloride stimulated the oxidation of NADH in the MPO-H2O2 system in a concentration-dependent manner (50-fold at 150 mM NaCl). Chlorides 0-8 myeloperoxidase Homo sapiens 49-52 1846732-7 1991 All changes observed with the myeloperoxidase system were inhibited by azide or methionine, and were dependent upon the presence of chloride, indicating that they are mediated by HOCl. Chlorides 132-140 myeloperoxidase Homo sapiens 30-45 2172341-1 1990 Neutrophil myeloperoxidase (MPO) adsorbs to bacteria as a pre-requisite for killing by the MPO/hydrogen-peroxide/chloride system. Chlorides 113-121 myeloperoxidase Homo sapiens 28-31 2172341-1 1990 Neutrophil myeloperoxidase (MPO) adsorbs to bacteria as a pre-requisite for killing by the MPO/hydrogen-peroxide/chloride system. Chlorides 113-121 myeloperoxidase Homo sapiens 91-94