PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1651573-2 1991 To determine the cytotoxicity of myeloperoxidase-generated oxygen metabolites (mainly chlorinated oxidants such as hypochlorite) and catechol oxidation products, the well characterized erythrocyte was used as a target. Oxygen 59-65 myeloperoxidase Homo sapiens 33-48 1654782-9 1991 These results therefore suggest that the interaction of phenolic compounds, presumably by hydrogen-bonding, with the activity limiting distal amino acid residue(s) or with the ferryl oxygen of peroxidase may be an important contributing factor in the enhanced myeloperoxidase-dependent metabolism of hydroquinone in the presence of other phenolic compounds. Oxygen 183-189 myeloperoxidase Homo sapiens 260-275 1311041-9 1992 The toxic oxygen species produced by this system caused lysis of the epithelial targets which was dependent on the duration of incubation and the concentrations of MPO and GO. Oxygen 10-16 myeloperoxidase Homo sapiens 164-167 1311041-13 1992 Furthermore, PMN MPO is capable of generating toxic oxygen species which can lyse these epithelial cells. Oxygen 52-58 myeloperoxidase Homo sapiens 17-20 1965118-1 1990 Neutrophil myeloperoxidase is an important component of the oxygen-dependent microbicidal system and is enzymatically activated in crevicular cells. Oxygen 60-66 myeloperoxidase Homo sapiens 11-26 1965503-1 1990 Myeloperoxidase (MPO) plays an important role in the oxygen-dependent microbicidal mechanism of polymorphonuclear neutrophils. Oxygen 53-59 myeloperoxidase Homo sapiens 0-15 1965503-1 1990 Myeloperoxidase (MPO) plays an important role in the oxygen-dependent microbicidal mechanism of polymorphonuclear neutrophils. Oxygen 53-59 myeloperoxidase Homo sapiens 17-20 1503677-4 1992 Drug oxidation by myeloperoxidase leads to free radical metabolite formation; these reactive free radicals can oxidise glutathione to a thiyl free radical, which in the presence of oxygen forms oxygen-derived free radicals. Oxygen 181-187 myeloperoxidase Homo sapiens 18-33 2162582-7 1990 The second reaction group was exemplified by human leucocyte myeloperoxidase which generated hypochlorite along with the active forms of oxygen. Oxygen 137-143 myeloperoxidase Homo sapiens 61-76 2162582-9 1990 The Ames test revealed mutagenic effects of the active oxygen forms generated by myeloperoxidase. Oxygen 55-61 myeloperoxidase Homo sapiens 81-96 1503677-4 1992 Drug oxidation by myeloperoxidase leads to free radical metabolite formation; these reactive free radicals can oxidise glutathione to a thiyl free radical, which in the presence of oxygen forms oxygen-derived free radicals. Oxygen 194-200 myeloperoxidase Homo sapiens 18-33 34535266-6 2021 O2 - production was synchronized with myeloperoxidase (MPO) activation in the former type but not in the latter. Oxygen 0-4 myeloperoxidase Homo sapiens 38-53 34535266-6 2021 O2 - production was synchronized with myeloperoxidase (MPO) activation in the former type but not in the latter. Oxygen 0-4 myeloperoxidase Homo sapiens 55-58 35020757-9 2022 This study suggests that while oxygen transport capacity is the main determinant of MPO regardless of sex, thigh muscle size also has a role in whole-body maximal aerobic performance in female athletes. Oxygen 31-37 myeloperoxidase Homo sapiens 84-87 2550701-3 1989 The role of MPO and its possible pathogenetic action as a generator of the active forms of oxygen in atherosclerosis and its complications has been discussed. Oxygen 91-97 myeloperoxidase Homo sapiens 12-15 2560462-7 1989 Inhibition by sodium azide and sodium benzoate indicated that these oxygen metabolites could be derived from the MPO-halide system but also from hydroxyl radical production. Oxygen 68-74 myeloperoxidase Homo sapiens 113-116 2552754-2 1989 Near-IR emission spectra from the myeloperoxidase and lactoperoxidase enzymatic systems show only emission of singlet oxygen at 1268 nm. Oxygen 118-124 myeloperoxidase Homo sapiens 34-49 2551812-1 1989 Myeloperoxidase (MPO), present in the azurophilic granules of human polymorphonuclear neutrophils, is important in the oxygen-dependent microbicidal activity of neutrophils. Oxygen 119-125 myeloperoxidase Homo sapiens 0-15 2540860-1 1989 Myeloperoxidase (MPO) is a heme containing enzyme involved in the oxygen-dependent microbicidal activity of human polymorphonuclear leukocytes (PMN). Oxygen 66-72 myeloperoxidase Homo sapiens 0-15 2540860-1 1989 Myeloperoxidase (MPO) is a heme containing enzyme involved in the oxygen-dependent microbicidal activity of human polymorphonuclear leukocytes (PMN). Oxygen 66-72 myeloperoxidase Homo sapiens 17-20 2540843-2 1989 As in the case of phenylacetaldehyde, the Schiff base undergoes an intracellular, myeloperoxidase-catalyzed, oxygen-consuming process. Oxygen 109-115 myeloperoxidase Homo sapiens 82-97 2551812-1 1989 Myeloperoxidase (MPO), present in the azurophilic granules of human polymorphonuclear neutrophils, is important in the oxygen-dependent microbicidal activity of neutrophils. Oxygen 119-125 myeloperoxidase Homo sapiens 17-20 2852003-3 1988 These minute amounts of reduced oxygen species are suggested to account for the initiation of myeloperoxidase-oxidase oxidation of thiols. Oxygen 32-38 myeloperoxidase Homo sapiens 94-109 2462938-1 1989 Myeloperoxidase (MPO) is a critical component in the oxygen-dependent microbicidal activity of neutrophils. Oxygen 53-59 myeloperoxidase Homo sapiens 0-15 2462938-1 1989 Myeloperoxidase (MPO) is a critical component in the oxygen-dependent microbicidal activity of neutrophils. Oxygen 53-59 myeloperoxidase Homo sapiens 17-20 2852003-5 1988 However, myeloperoxidase-mediated oxidation of thiols with concomitant O2 consumption can also occur with myeloperoxidase in its Compound II oxidation state. Oxygen 71-73 myeloperoxidase Homo sapiens 9-24 2852003-5 1988 However, myeloperoxidase-mediated oxidation of thiols with concomitant O2 consumption can also occur with myeloperoxidase in its Compound II oxidation state. Oxygen 71-73 myeloperoxidase Homo sapiens 106-121 2855142-0 1988 [Active oxygen production in myeloperoxidase system]. Oxygen 8-14 myeloperoxidase Homo sapiens 29-44 6090316-4 1984 The oxygen-dependent brucellacidal activity of granule extracts was dependent on concentrations of myeloperoxidase (MPO) units, H2O2, and KI. Oxygen 4-10 myeloperoxidase Homo sapiens 99-114 2828362-11 1988 This activity is blocked by superoxide dismutase but does not require O2- production by the NADPH-oxidase, indicating that myeloperoxidase produces O2- when incubated with RSH compounds. Oxygen 148-150 myeloperoxidase Homo sapiens 123-138 2831080-2 1988 Optimal oxygen-dependent microbicidal activity depends on MPO as the critical enzyme for the generation of hypochlorous acid and other toxic oxygen products. Oxygen 8-14 myeloperoxidase Homo sapiens 58-61 2831080-2 1988 Optimal oxygen-dependent microbicidal activity depends on MPO as the critical enzyme for the generation of hypochlorous acid and other toxic oxygen products. Oxygen 141-147 myeloperoxidase Homo sapiens 58-61 2822673-5 1987 Myeloperoxidase compound I reacted with H2O2 and returned to the ferric state with concomitant evolution of an O2 molecule. Oxygen 42-44 myeloperoxidase Homo sapiens 0-15 3030427-7 1987 Concomitantly, Compound I of myeloperoxidase would be reduced to Compound II and superoxide anions would be generated from oxygen. Oxygen 123-129 myeloperoxidase Homo sapiens 29-44 2981925-3 1985 Neutrophils and other phagocytes can injure cells by means of oxygen-dependent mechanisms, particularly the myeloperoxidase (MPO)-H2O2-halide system. Oxygen 62-68 myeloperoxidase Homo sapiens 108-123 2981925-3 1985 Neutrophils and other phagocytes can injure cells by means of oxygen-dependent mechanisms, particularly the myeloperoxidase (MPO)-H2O2-halide system. Oxygen 62-68 myeloperoxidase Homo sapiens 125-128 2829220-9 1988 These data suggest that intranuclear MPO may help to protect DNA against damage resulting from oxygen radicals produced during myeloid cell maturation and function. Oxygen 95-101 myeloperoxidase Homo sapiens 37-40 2820530-1 1987 Myeloperoxidase (MPO) is a lysosomal enzyme present in the azurophilic granules of human neutrophils and monocytes and is important for optimal oxygen-dependent killing of microorganisms. Oxygen 144-150 myeloperoxidase Homo sapiens 0-15 2820530-1 1987 Myeloperoxidase (MPO) is a lysosomal enzyme present in the azurophilic granules of human neutrophils and monocytes and is important for optimal oxygen-dependent killing of microorganisms. Oxygen 144-150 myeloperoxidase Homo sapiens 17-20 3039546-2 1987 In polymorphonuclear leukocytes phenylacetaldehyde promotes an intracellular O2 consuming process in which myeloperoxidase participates. Oxygen 77-79 myeloperoxidase Homo sapiens 107-122 2822673-4 1987 As for the latter, true catalase activity of myeloperoxidase was demonstrated by monitoring O2 evolution after the injection of H2O2 into the enzyme solution. Oxygen 92-94 myeloperoxidase Homo sapiens 45-60 3021423-0 1986 [Inactivation of active forms of oxygen generated by myeloperoxidase and serum proteins]. Oxygen 33-39 myeloperoxidase Homo sapiens 53-68 6090316-4 1984 The oxygen-dependent brucellacidal activity of granule extracts was dependent on concentrations of myeloperoxidase (MPO) units, H2O2, and KI. Oxygen 4-10 myeloperoxidase Homo sapiens 116-119 6297637-1 1983 Myeloperoxidase (MPO), a heme enzyme present in the primary granules of polymorphonuclear leukocytes (PMNs), has been demonstrated to participate in the oxygen-dependent microbicidal activity of these cells. Oxygen 153-159 myeloperoxidase Homo sapiens 0-15 6487320-1 1984 A method for investigating the cellular response of polymorphonuclear leukocytes to various stimuli was introduced using simultaneously native (luminol-independent) and luminol dependent luminescence as an indicator for myeloperoxidase (MPO)-H2O2-halide and O2- mediated reactions. Oxygen 244-246 myeloperoxidase Homo sapiens 220-235 6487320-1 1984 A method for investigating the cellular response of polymorphonuclear leukocytes to various stimuli was introduced using simultaneously native (luminol-independent) and luminol dependent luminescence as an indicator for myeloperoxidase (MPO)-H2O2-halide and O2- mediated reactions. Oxygen 244-246 myeloperoxidase Homo sapiens 237-240 6487320-3 1984 Consequently the MPO-H2O2-halide system could be distinguished from the O2- dependent system by interpreting the recorded temporal traces of the emitted light. Oxygen 23-25 myeloperoxidase Homo sapiens 17-20 6087808-0 1984 Myeloperoxidase singlet molecular oxygen generation detected by direct infrared electronic emission. Oxygen 34-40 myeloperoxidase Homo sapiens 0-15 6321594-2 1984 Demonstration of an oxygen-dependent myeloperoxidase-independent mechanism. Oxygen 20-26 myeloperoxidase Homo sapiens 37-52 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. Oxygen 26-32 myeloperoxidase Homo sapiens 153-168 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. Oxygen 34-36 myeloperoxidase Homo sapiens 153-168 6189859-1 1983 Myeloperoxidase (MPO), a heme enzyme present in the azurophilic granules of human polymorphonuclear neutrophils (PMN), is important in the oxygen-dependent microbicidal activity of PMN. Oxygen 139-145 myeloperoxidase Homo sapiens 0-15 6189859-1 1983 Myeloperoxidase (MPO), a heme enzyme present in the azurophilic granules of human polymorphonuclear neutrophils (PMN), is important in the oxygen-dependent microbicidal activity of PMN. Oxygen 139-145 myeloperoxidase Homo sapiens 17-20 6297637-1 1983 Myeloperoxidase (MPO), a heme enzyme present in the primary granules of polymorphonuclear leukocytes (PMNs), has been demonstrated to participate in the oxygen-dependent microbicidal activity of these cells. Oxygen 153-159 myeloperoxidase Homo sapiens 17-20 6297637-4 1983 The role of MPO in PMN oxygen metabolism was examined by studying parameters of the respiratory burst of PMNs from a number of unrelated MPO-deficient subjects; in addition, the ability of heme enzyme inhibitors to duplicate the MPO-deficient state was studied by treating normal and MPO-deficient cells with these compounds. Oxygen 23-29 myeloperoxidase Homo sapiens 12-15 12111-4 1976 A peptide chloromethyl ketone elastase inhibitor abolished both elastolytic activity and the pctentiating effects on MPO-H2-O2-mediated bacterial killing. Oxygen 124-126 myeloperoxidase Homo sapiens 117-120 7062313-7 1982 Results suggested that the phagocytic CL response in our assay system was dependent on O2 activation followed by the activated O2 species reacting with myeloperoxidase and chloride. Oxygen 127-129 myeloperoxidase Homo sapiens 152-167 225142-9 1978 The MPO-independent antimicrobial systems may be oxygen-dependent or oxygen-independent. Oxygen 49-55 myeloperoxidase Homo sapiens 4-7 225142-9 1978 The MPO-independent antimicrobial systems may be oxygen-dependent or oxygen-independent. Oxygen 69-75 myeloperoxidase Homo sapiens 4-7 207730-5 1978 Exposure to zymosan under conditions in which the myeloperoxidase system was inactive (i.e., in the presence of myeloperoxidase inhibitors, or in the absence of oxygen) resulted in a substantial increase in the initial O(2) (-)-forming activity of particles from the zymosan-treated cells, but did not prevent the sharp fall in activity seen when zymosan exposure exceeded 10 min. Oxygen 219-225 myeloperoxidase Homo sapiens 50-65 7219526-6 1981 Activation of the oxidase is associated with the generation of various reduced oxygen species which have been widely thought to be responsible for the killing of phagocytosed microorganisms either directly, or by acting as substrates for myeloperoxidase-mediated halogenation. Oxygen 79-85 myeloperoxidase Homo sapiens 238-253 193132-4 1977 Some of the systems that depend on oxygen also require myeloperoxidase. Oxygen 35-41 myeloperoxidase Homo sapiens 55-70 21895822-9 2012 All inflammatory markers except MPO correlated to AHI and oxygen desaturation measures, and to waist circumference. Oxygen 58-64 myeloperoxidase Homo sapiens 32-35 26137956-2 2015 Myeloperoxidase is a reactive oxygen generating enzyme and is expressed by microglia. Oxygen 30-36 myeloperoxidase Homo sapiens 0-15 22855218-7 2012 During strenuous exercising, MPO as well as its educts may be elevated due to increased oxygen intake and excretion of pro-inflammatory mediators inducing host tissue damage via oxidative stress. Oxygen 88-94 myeloperoxidase Homo sapiens 29-32 31879336-1 2020 BACKGROUND: Myeloperoxidase released after neutrophil and monocyte activation can generate reactive oxygen species, leading to host tissue damage. Oxygen 100-106 myeloperoxidase Homo sapiens 12-27 29975476-1 2016 The purpose of this work was to define dependence of maintenance of myeloperoxidase (MPO) in plasma of blood of patients by the acute infarct of myocardium from the state of oxygen metabolism of neutrophils, which was estimated on activity of myeloperoxidases, superoxid-anion and catalase in cells and on maintenance by peroxigens. Oxygen 174-180 myeloperoxidase Homo sapiens 68-83 29975476-1 2016 The purpose of this work was to define dependence of maintenance of myeloperoxidase (MPO) in plasma of blood of patients by the acute infarct of myocardium from the state of oxygen metabolism of neutrophils, which was estimated on activity of myeloperoxidases, superoxid-anion and catalase in cells and on maintenance by peroxigens. Oxygen 174-180 myeloperoxidase Homo sapiens 85-88 26719776-2 2015 Myeloperoxidase plays an important role in oxygen-dependent killing of bacteria, fungi, virus and malignant cells. Oxygen 43-49 myeloperoxidase Homo sapiens 0-15 26170654-10 2015 Among patients with low transcutaneous oxygen saturation during exacerbations, PaO2 (partial oxygen pressure) correlated with concentrations of MPO and NE protein and neutrophils in a negative manner. Oxygen 39-45 myeloperoxidase Homo sapiens 144-147 26170654-10 2015 Among patients with low transcutaneous oxygen saturation during exacerbations, PaO2 (partial oxygen pressure) correlated with concentrations of MPO and NE protein and neutrophils in a negative manner. Oxygen 93-99 myeloperoxidase Homo sapiens 144-147 19760108-7 2010 Higher concentrations of zinc results on a rapid dismutation of O2*- to oxygen and hydrogen peroxide, which in turn is used by myeloperoxidase to generate hypochlorous acid (HOCl). Oxygen 64-66 myeloperoxidase Homo sapiens 127-142 22143159-4 2012 The classic paradigm views MPO as a component of the phagocyte oxygen-dependent intracellular microbicidal system, and thus an important arm of the effector phase of innate immune responses. Oxygen 63-69 myeloperoxidase Homo sapiens 27-30 19760108-7 2010 Higher concentrations of zinc results on a rapid dismutation of O2*- to oxygen and hydrogen peroxide, which in turn is used by myeloperoxidase to generate hypochlorous acid (HOCl). Oxygen 72-78 myeloperoxidase Homo sapiens 127-142 19506990-13 2009 This MPO, which releases proteolytic enzymes and radical oxygen species, acts on tissue destruction, namely the lysis of endothelial cell membranes as well as vascular basement membranes in the peritubular capillary. Oxygen 57-63 myeloperoxidase Homo sapiens 5-8 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. Oxygen 152-158 myeloperoxidase Homo sapiens 21-24 19877306-1 2009 OBJECTIVE: Myeloperoxidase catalyzes the formation of reactive oxygen metabolites in neutrophils and monocytes. Oxygen 63-69 myeloperoxidase Homo sapiens 11-26 19298750-6 2009 CONCLUSION: On a molecular level, hyperbaric oxygen therapy leads to activation of ion channels, inhibition of hypoxia inducible factor-1alpha, up-regulation of Bcl-2, inhibition of MMP-9, decreased cyclooxygenase-2 activity, decreased myeloperoxidase activity, up-regulation of superoxide dismutase and inhibition of Nogo-A (an endogenous growth-inhibitory factor). Oxygen 45-51 myeloperoxidase Homo sapiens 236-251 19339248-7 2009 The site corresponding to the positions of Gln(423), Phe(422) oxygen, and Wat(6)" in LPO is occupied primarily by the side chain of Phe(407) in MPO due to an entirely different conformation of the loop corresponding to the segment Arg(418)-Phe(431) of LPO. Oxygen 62-68 myeloperoxidase Homo sapiens 144-147 18283105-2 2008 Results demonstrate that exposure to high oxygen partial pressures increases synthesis of reactive species derived from type 2 nitric-oxide synthase and myeloperoxidase, leading to excessive S-nitrosylation of beta-actin and possibly profilin. Oxygen 42-48 myeloperoxidase Homo sapiens 153-168 19950861-2 2009 It was shown that neopterin and 7, 8-dihydroneopterin while being a redox-pair regulated the process of oxygen activation in neutrophils by functioning of myeloperoxidase. Oxygen 104-110 myeloperoxidase Homo sapiens 155-170 16392333-6 2005 Impairment of the myeloperoxidase- and NADPH-depended production of active oxygen by non-activated and activated neutrophils observed before operations resulted in altered synthesis of active oxygen after the surgery. Oxygen 75-81 myeloperoxidase Homo sapiens 18-33 16148002-13 2005 In the other pathway, myeloperoxidase uses superoxide to insert dioxygen into melatonin to form AFMK. Oxygen 64-72 myeloperoxidase Homo sapiens 22-37 17381162-12 2007 These interactions of superoxide and myeloperoxidase will have a major influence on the way neutrophils use oxygen to kill bacteria. Oxygen 108-114 myeloperoxidase Homo sapiens 37-52 15464726-1 2004 We have studied the peroxidase-oxidase reaction catalyzed by human myeloperoxidase in an open system where both substrates-molecular oxygen and NADH-are supplied continuously to the reaction mixture. Oxygen 133-139 myeloperoxidase Homo sapiens 67-82 12711384-3 2003 According to our results, when 50% of the peroxidase activity in saliva was due to MPO, determined using a typical substrate for peroxidase guaiacol, almost all oxygen evolved was due to SPX. Oxygen 161-167 myeloperoxidase Homo sapiens 83-86 15600254-9 2004 Myeloperoxidase (MPD) is a heme enzyme, participating in oxygen mechanisms of microorganism killing by phagocytes. Oxygen 57-63 myeloperoxidase Homo sapiens 0-15 16392333-6 2005 Impairment of the myeloperoxidase- and NADPH-depended production of active oxygen by non-activated and activated neutrophils observed before operations resulted in altered synthesis of active oxygen after the surgery. Oxygen 192-198 myeloperoxidase Homo sapiens 18-33 16392333-8 2005 Detection of the myeloperoxidase- and NADPH-depended production of active oxygen could be of help in revealing the groups of risk among patients at the stage of the preoperative examination and serve as a prognostic factor of the development of severe infectious complications during the postoperative period. Oxygen 74-80 myeloperoxidase Homo sapiens 17-32 15350145-0 2004 A novel multistep mechanism for oxygen binding to ferrous hemoproteins: rapid kinetic analysis of ferrous-dioxy myeloperoxidase (compound III) formation. Oxygen 32-38 myeloperoxidase Homo sapiens 112-127 15350145-4 2004 Using spectral and rapid kinetic measurements, we now demonstrate that molecular oxygen (O(2)) binds to ferrous MPO (MPO-Fe(II)) in a distinct and novel mechanism. Oxygen 81-87 myeloperoxidase Homo sapiens 112-115 15350145-4 2004 Using spectral and rapid kinetic measurements, we now demonstrate that molecular oxygen (O(2)) binds to ferrous MPO (MPO-Fe(II)) in a distinct and novel mechanism. Oxygen 81-87 myeloperoxidase Homo sapiens 117-127 15350145-4 2004 Using spectral and rapid kinetic measurements, we now demonstrate that molecular oxygen (O(2)) binds to ferrous MPO (MPO-Fe(II)) in a distinct and novel mechanism. Oxygen 89-94 myeloperoxidase Homo sapiens 112-115 15350145-4 2004 Using spectral and rapid kinetic measurements, we now demonstrate that molecular oxygen (O(2)) binds to ferrous MPO (MPO-Fe(II)) in a distinct and novel mechanism. Oxygen 89-94 myeloperoxidase Homo sapiens 117-127 15350145-8 2004 Insights into mechanisms for inactivating MPO and the novel mode of O(2) binding to the hemoprotein may provide important clues toward understanding the catalytic action of MPO. Oxygen 68-72 myeloperoxidase Homo sapiens 173-176 15130787-0 2004 Kinetics of oxygen binding to ferrous myeloperoxidase. Oxygen 12-18 myeloperoxidase Homo sapiens 38-53 15130787-3 2004 To investigate the reactivity of ferrous MPO with molecular oxygen, a stopped-flow kinetic analysis was performed. Oxygen 60-66 myeloperoxidase Homo sapiens 41-44 15130787-5 2004 At pH 7.0 and 25 degrees C, compound III formation (i.e., binding of dioxygen to ferrous MPO) occurs with a rate constant of (1.1+/-0.1) x 10(4)M(-1)s(-1). Oxygen 69-77 myeloperoxidase Homo sapiens 89-92 15130787-8 2004 The rate constant of dioxygen dissociation from compound III is much higher than conversion of compound III to ferric MPO (which is not affected by the oxygen concentration). Oxygen 23-29 myeloperoxidase Homo sapiens 118-121 12524266-3 2003 The model predicts that after activation of a neutrophil, an increase in the activity of the hexose monophosphate shunt and the delivery of myeloperoxidase into the phagosome results in oscillations in oxygen and NAD(P)H concentration. Oxygen 202-208 myeloperoxidase Homo sapiens 140-155 12816056-6 2003 O2.- is also a physiological substrate of myeloperoxidase. Oxygen 0-2 myeloperoxidase Homo sapiens 42-57 12816056-8 2003 O2.- affects the chlorinating and peroxidase activities of myeloperoxidase. Oxygen 0-2 myeloperoxidase Homo sapiens 59-74 12953846-1 2003 The microbicidal activity of the myeloperoxidase (MPO)-hydrogen peroxide-halide system has been implicated as the most efficient, oxygen-dependent antimicrobial component of neutrophil host defense. Oxygen 130-136 myeloperoxidase Homo sapiens 33-48 12953846-1 2003 The microbicidal activity of the myeloperoxidase (MPO)-hydrogen peroxide-halide system has been implicated as the most efficient, oxygen-dependent antimicrobial component of neutrophil host defense. Oxygen 130-136 myeloperoxidase Homo sapiens 50-53 11594511-1 2001 Optimal oxygen-dependent antimicrobial activity of circulating polymorphonuclear leukocytes reflects the synergistic effects of the myeloperoxidase (MPO)-hydrogen peroxide-halide system. Oxygen 8-14 myeloperoxidase Homo sapiens 132-147 12071050-1 2002 Myeloperoxidase plays the key role in antimicrobial oxygen-dependent activity of neutrophils. Oxygen 52-58 myeloperoxidase Homo sapiens 0-15 11594511-1 2001 Optimal oxygen-dependent antimicrobial activity of circulating polymorphonuclear leukocytes reflects the synergistic effects of the myeloperoxidase (MPO)-hydrogen peroxide-halide system. Oxygen 8-14 myeloperoxidase Homo sapiens 149-152 10994872-7 2000 We could monitor formation of ferrous myeloperoxidase as well as its direct transition to compound II by addition of molecular oxygen. Oxygen 127-133 myeloperoxidase Homo sapiens 38-53 10742562-1 2000 Myeloperoxidase (MPO) generates hypochlorous acid and other reactive oxygen intermediates leading to tissue damage. Oxygen 69-75 myeloperoxidase Homo sapiens 0-15 10742562-1 2000 Myeloperoxidase (MPO) generates hypochlorous acid and other reactive oxygen intermediates leading to tissue damage. Oxygen 69-75 myeloperoxidase Homo sapiens 17-20 10677352-17 2000 Most importantly, incubation of apo A-I with the myeloperoxidase/H(2)O(2)/Cl(-) system (the source of HOCl in vivo) resulted in almost identical modification patterns to those observed with reagent NaOCl. Oxygen 69-73 myeloperoxidase Homo sapiens 49-64 10658829-8 2000 The O2 and O2+NO groups did not differ in CD18 expression or in intracellular oxidant production, but had significant increase in lung myeloperoxidase compared to the RA group. Oxygen 4-6 myeloperoxidase Homo sapiens 135-150 10482305-1 1999 The optimal level of oxygen-dependent microbicidal activity in human neutrophils depends on the generation of highly toxic products, including hypochlorous acid, by hydrogen peroxide in the presence of chloride anion and the neutrophil granule protein myeloperoxidase (MPO). Oxygen 21-27 myeloperoxidase Homo sapiens 252-267 10482305-1 1999 The optimal level of oxygen-dependent microbicidal activity in human neutrophils depends on the generation of highly toxic products, including hypochlorous acid, by hydrogen peroxide in the presence of chloride anion and the neutrophil granule protein myeloperoxidase (MPO). Oxygen 21-27 myeloperoxidase Homo sapiens 269-272 10226494-4 1999 The course of the ozone-oxygen irrigations produced good results: ear discharge and tympanic mucosa inflammation stopped in 81% of the irrigated patients, levels of myeloperoxidase which marks inflammation reduced significantly, bactericidal effects of the mixture were observed for all the detected pathogens, antibiotic sensitivity of the bacteria rose. Oxygen 24-30 myeloperoxidase Homo sapiens 165-180 10450791-6 1999 CONCLUSIONS: These results suggest that elevated levels of insulin do not affect the NADPH-oxidase activity but, together with superoxide anions, interfere with myeloperoxidase availability and a subsequent myeloperoxidase-dependent generation of reactive oxygen metabolites in fMet-Leu-Phe-stimulated normal human neutrophils. Oxygen 256-262 myeloperoxidase Homo sapiens 207-222 9989595-0 1999 Physiological production of singlet molecular oxygen in the myeloperoxidase-H2O2-chloride system. Oxygen 28-52 myeloperoxidase Homo sapiens 60-75 10498986-1 1999 Experiments on 25 intact dogs, 2 calves and clinical tests in 45 patients have shown that in the blood of the aorta or pulmonary vein leaving the lungs there is a rise in generation of active oxygen forms by leukocytes, their phagocytic activity, the activity of myeloperoxidase, NADPN-oxidase, complement, immunoglobulins content. Oxygen 192-198 myeloperoxidase Homo sapiens 263-278 9766845-2 1998 Despite the primary role of the oxygen-dependent MPO system in the destruction of certain phagocytosed microbes, subjects with total or partial MPO deficiency generally do not have an increased frequency of infections, probably because other MPO-independent mechanism(s) for microbicidal activity compensate for the lack of MPO. Oxygen 32-38 myeloperoxidase Homo sapiens 49-52 9507022-1 1998 Myeloperoxidase (MPO) is a neutrophil lysosomal hemeprotein essential for optimal oxygen-dependent microbicidal activity. Oxygen 82-88 myeloperoxidase Homo sapiens 0-15 9507022-1 1998 Myeloperoxidase (MPO) is a neutrophil lysosomal hemeprotein essential for optimal oxygen-dependent microbicidal activity. Oxygen 82-88 myeloperoxidase Homo sapiens 17-20 9468538-1 1998 Myeloperoxidase (MPO), stored in azurophil granules of neutrophils, is critical for an optimal oxygen-dependent microbicidal activity of these cells. Oxygen 95-101 myeloperoxidase Homo sapiens 17-20 9128147-1 1997 Myeloperoxidase (MPO), an important enzyme in the oxygen-dependent host defense system of human polymorphonuclear leukocytes, utilizes hydrogen peroxide to catalyze the production of hypochlorous acid, an oxidizing bactericidal agent. Oxygen 50-56 myeloperoxidase Homo sapiens 0-15 9791941-13 1998 This indicates that in the bacterium/neutrophilic granulocyte system oxygen metabolites are generated that are capable of reacting with MPO. Oxygen 69-75 myeloperoxidase Homo sapiens 136-139 9468538-1 1998 Myeloperoxidase (MPO), stored in azurophil granules of neutrophils, is critical for an optimal oxygen-dependent microbicidal activity of these cells. Oxygen 95-101 myeloperoxidase Homo sapiens 0-15 9551742-2 1998 It is based on the assumption that neutrophils entering the lumen of the infected airways undergo activation and release toxic oxygen metabolites and myeloperoxidase (MPO), an enzyme which transforms hydrogen peroxide (H2O2) into highly toxic oxygen metabolites. Oxygen 243-249 myeloperoxidase Homo sapiens 150-165 9551742-2 1998 It is based on the assumption that neutrophils entering the lumen of the infected airways undergo activation and release toxic oxygen metabolites and myeloperoxidase (MPO), an enzyme which transforms hydrogen peroxide (H2O2) into highly toxic oxygen metabolites. Oxygen 243-249 myeloperoxidase Homo sapiens 167-170 9468285-1 1998 Myeloperoxidase (MPO) is an essential component of the oxygen-dependent microbicidal system of neutrophils and monocytes. Oxygen 55-61 myeloperoxidase Homo sapiens 0-15 9468285-1 1998 Myeloperoxidase (MPO) is an essential component of the oxygen-dependent microbicidal system of neutrophils and monocytes. Oxygen 55-61 myeloperoxidase Homo sapiens 17-20 9128147-1 1997 Myeloperoxidase (MPO), an important enzyme in the oxygen-dependent host defense system of human polymorphonuclear leukocytes, utilizes hydrogen peroxide to catalyze the production of hypochlorous acid, an oxidizing bactericidal agent. Oxygen 50-56 myeloperoxidase Homo sapiens 17-20 7772042-7 1995 Thus it is likely that hydrogen-bonding of the enzyme to substituents containing oxygen or nitrogen increases the binding affinity of the hydrazides and enhances their oxidation by myeloperoxidase. Oxygen 81-87 myeloperoxidase Homo sapiens 181-196 9020887-9 1997 In the presence of oxygen, ABAH and hydrogen peroxide initially converted myeloperoxidase into compound III, which subsequently lost haem absorbance. Oxygen 19-25 myeloperoxidase Homo sapiens 74-89 9020887-10 1997 In the absence of oxygen, the enzyme was converted into ferrous myeloperoxidase and its haem groups were rapidly destroyed. Oxygen 18-24 myeloperoxidase Homo sapiens 64-79 9020887-12 1997 Ferrous myeloperoxidase reacts either with oxygen to allow enzyme turnover, or with hydrogen peroxide to give irreversible inactivation. Oxygen 43-49 myeloperoxidase Homo sapiens 8-23 8751892-0 1996 Involvement of superoxide and myeloperoxidase in oxygen-dependent killing of Staphylococcus aureus by neutrophils. Oxygen 49-55 myeloperoxidase Homo sapiens 30-45 8718890-6 1996 The ability of the three SHA oxygen atoms to closely duplicate the hydrogen-bonding pattern of these three water molecules in the native enzyme is postulated to account for the strong binding of this inhibitor to MPO. Oxygen 29-35 myeloperoxidase Homo sapiens 213-216 8621627-1 1996 Human neutrophil microbicidal activity is largely mediated by reactive species generated by the oxygen-dependent myeloperoxidase (MPO) system. Oxygen 96-102 myeloperoxidase Homo sapiens 113-128 8621627-1 1996 Human neutrophil microbicidal activity is largely mediated by reactive species generated by the oxygen-dependent myeloperoxidase (MPO) system. Oxygen 96-102 myeloperoxidase Homo sapiens 130-133 8605038-4 1996 These results suggest that MP plays a role as an absorber of active oxygen species and prevents phagocytes from self-destruction. Oxygen 68-74 myeloperoxidase Homo sapiens 27-29 7649486-3 1995 We present a simple method for the differentiation between oxygen activating reactions in which neutrophil-derived myeloperoxidase is involved. Oxygen 59-65 myeloperoxidase Homo sapiens 115-130 8604000-6 1996 Our results also indicate that specific and azurophil granules have to be in very close contact to allow the generated oxygen metabolites to reach and react with myeloperoxidase. Oxygen 119-125 myeloperoxidase Homo sapiens 162-177 7876246-1 1995 Myeloperoxidase (MPO), a lysosomal heme protein found exclusively in neutrophils and monocytes, is necessary for efficient oxygen-dependent microbicidal activity. Oxygen 123-129 myeloperoxidase Homo sapiens 0-15 7876246-1 1995 Myeloperoxidase (MPO), a lysosomal heme protein found exclusively in neutrophils and monocytes, is necessary for efficient oxygen-dependent microbicidal activity. Oxygen 123-129 myeloperoxidase Homo sapiens 17-20 7776904-8 1995 We propose that the release of MyPo from neutrophils and subsequent binding to macrophages initiates a cascade of events which enhance the production of reactive oxygen intermediates and cytokine expression resulting in the chronic inflammatory state associated with autoimmune diseases. Oxygen 162-168 myeloperoxidase Homo sapiens 31-35 8147902-3 1994 An intermediate of isoniazid reduced ferric MPO to ferrous MPO which associated with dioxygen to form compound III. Oxygen 85-93 myeloperoxidase Homo sapiens 44-47 8147902-3 1994 An intermediate of isoniazid reduced ferric MPO to ferrous MPO which associated with dioxygen to form compound III. Oxygen 85-93 myeloperoxidase Homo sapiens 59-62 8147902-11 1994 In addition, phytic acid also facilitated compound III decay in the absence of isoniazid, suggesting that it may also regulate the oxygen affinity of MPO, similar to its effect on the oxygenation of haemoglobin. Oxygen 131-137 myeloperoxidase Homo sapiens 150-153 8385264-3 1993 We investigated the oxygen-dependent bactericidal activities including the ability to generate O2-, Myeloperoxidase (MPO) activity and opsonic activity using chemiluminescence method. Oxygen 20-26 myeloperoxidase Homo sapiens 100-115 8177196-8 1994 These results suggest that postoperative PMN signal transduction mechanisms, mediated by protein kinase C, may activate myeloperoxidase-H2-O2-halide system but suppress NADPH oxidase system dependently of the degree of surgical stress, revealing a differential effect of protein kinase C activation on PMN microbicidal activity. Oxygen 139-141 myeloperoxidase Homo sapiens 120-135 8395934-0 1993 Formation of a hydroxyl radical by the myeloperoxidase-NADH-oxygen system. Oxygen 60-66 myeloperoxidase Homo sapiens 39-54 8395934-6 1993 Even though the superoxide radical (O2-)-producing ability of the MPO-NADH system was about 29% of that of the hypoxanthine-xanthine oxidase system, under the experimental conditions employed, the rate of tyrosine formation from phenylalanine by two systems was found to be a similar. Oxygen 36-38 myeloperoxidase Homo sapiens 66-69 8385264-3 1993 We investigated the oxygen-dependent bactericidal activities including the ability to generate O2-, Myeloperoxidase (MPO) activity and opsonic activity using chemiluminescence method. Oxygen 20-26 myeloperoxidase Homo sapiens 117-120 1338273-6 1992 The results suggest that O2- might be scavenged both directly by iodination stimulators, and by other oxygen radicals produced by activation of myeloperoxidase-mediated reaction. Oxygen 25-27 myeloperoxidase Homo sapiens 144-159 8469893-4 1993 Macrophages/monocytes and polymorphonuclear leucocytes produce then active oxygen species and cytokines; they degranulate (releasing active enzymes such as myeloperoxidase), they express an increasing number of membrane receptors able to interact with endothelial cells and release a supplementary lot of inflammatory mediators (prostanoids, platelet activating factor, leukotrienes ... ). Oxygen 75-81 myeloperoxidase Homo sapiens 156-171 1330078-1 1992 Biosynthesis of myeloperoxidase (MPO), a myeloid lysosomal hemoprotein critical for the optimal oxygen-dependent microbicidal activity of human neutrophils, is incompletely understood. Oxygen 96-102 myeloperoxidase Homo sapiens 16-31 1330078-1 1992 Biosynthesis of myeloperoxidase (MPO), a myeloid lysosomal hemoprotein critical for the optimal oxygen-dependent microbicidal activity of human neutrophils, is incompletely understood. Oxygen 96-102 myeloperoxidase Homo sapiens 33-36