PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19850004-7 2010 Genomic DNA recovered from E. coli that had been subjected to phagocytosis by human neutrophils occasionally showed small increases in 5-chlorocytosine content when compared to analogous cellular reactions where myeloperoxidase activity was inhibited by azide ion. Azides 254-259 myeloperoxidase Homo sapiens 212-227 16024637-4 2005 Methimazole, 4-aminobenzoic acid hydrazide, or azide inhibits the reaction, suggesting that it is mediated by the cellular myeloperoxidase, an enzyme naturally present in large amounts in HL-60 cells. Azides 37-42 myeloperoxidase Homo sapiens 123-138 15039448-7 2004 A thiol-blocking reagent, N-ethylmaleimide, as well as myeloperoxidase inhibitors (succinyl acetone and azide), blocked formation of fluorescent acridine-piperidine. Azides 104-109 myeloperoxidase Homo sapiens 55-70 15531583-13 2005 MPO nonnitrosative oxidation of IQ with 0.3 mm NO(2)(-) at pH 5.5 was inhibited by azide, but not NADH, demonstrating differences between MPO oxidation of IQ with NO compared with NO(2)(-). Azides 83-88 myeloperoxidase Homo sapiens 0-3 15203186-10 2004 MPO-mediated lipid oxidation was inhibited by heme poisons (azide, cyanide) and catalase. Azides 60-65 myeloperoxidase Homo sapiens 0-3 10602307-8 1999 The CL from ABEI-ms with hydrogen peroxide/MPO was completely inhibited by azide. Azides 75-80 myeloperoxidase Homo sapiens 43-46 12717622-5 2003 Coincubation with either catalase, with the myeloperoxidase inhibitor azide, or with the hypochlorous acid scavenger methionine almost completely prevented activation, but not the release, of MMP-9, in supernatants of human PMNs stimulated with hiR6. Azides 70-75 myeloperoxidase Homo sapiens 44-59 7762419-6 1995 Lucigenin-dependent CL of sulphite-treated and subsequently stimulated neutrophils was strongly inhibited by extracellularly added superoxide dismutase, whereas luminol-dependent CL was markedly reduced by the MPO inhibitor azide. Azides 224-229 myeloperoxidase Homo sapiens 210-213 8751892-3 1996 Myeloperoxidase was inhibited with azide, and myeloperoxidase-deficient neutrophils were used. Azides 35-40 myeloperoxidase Homo sapiens 0-15 10462537-9 1999 )radicals is completely blocked by myeloperoxidase inhibitors, cyanide and azide. Azides 89-94 myeloperoxidase Homo sapiens 49-64 10393704-8 1999 CML production by neutrophils was inhibited by the H2O2 scavenger catalase and the heme poison azide, implicating myeloperoxidase in the cell-mediated reaction. Azides 95-100 myeloperoxidase Homo sapiens 114-129 9660850-6 1998 No metabolism was detected in neutrophils that had not been activated, and the oxidation was inhibited by azide (which inhibits MPO) and by catalase (which catalyzes the breakdown of H2O2). Azides 106-111 myeloperoxidase Homo sapiens 128-131 9718094-4 1998 Azide can be oxidized by catalase and myeloperoxidase in the presence of H2O2, resulting in the generation of nitric oxide (NO). Azides 0-5 myeloperoxidase Homo sapiens 38-53 9718094-6 1998 Azide-induced migration, and the enhancement by azide of fMLP/CB-induced exocytosis, were blocked by pre-incubating cells with aminotriazole, an inhibitor of catalase and myeloperoxidase, suggesting that the effect of azide was mediated by NO. Azides 0-5 myeloperoxidase Homo sapiens 171-186 9718094-6 1998 Azide-induced migration, and the enhancement by azide of fMLP/CB-induced exocytosis, were blocked by pre-incubating cells with aminotriazole, an inhibitor of catalase and myeloperoxidase, suggesting that the effect of azide was mediated by NO. Azides 48-53 myeloperoxidase Homo sapiens 171-186 9034238-7 1997 The formation of 3-chloro PABA was inhibited by azide, catalase, and taurine, which is consistent with the production of the metabolite by the neutrophil myeloperoxidase (MPO) pathway. Azides 48-53 myeloperoxidase Homo sapiens 154-169 9034238-7 1997 The formation of 3-chloro PABA was inhibited by azide, catalase, and taurine, which is consistent with the production of the metabolite by the neutrophil myeloperoxidase (MPO) pathway. Azides 48-53 myeloperoxidase Homo sapiens 171-174 8877407-10 1996 Azide, an inhibitor of myeloperoxidase, and catalase which destroys H2O2, essential for MPO-catalyzed oxidations, prevented the generation of C5 activating potency and of chloramines. Azides 0-5 myeloperoxidase Homo sapiens 23-38 8877407-10 1996 Azide, an inhibitor of myeloperoxidase, and catalase which destroys H2O2, essential for MPO-catalyzed oxidations, prevented the generation of C5 activating potency and of chloramines. Azides 0-5 myeloperoxidase Homo sapiens 88-91 1352211-5 1992 Myeloperoxidase is likely the enzyme in the leukocyte involved, since the oxidation was inhibited by azide, which inhibits myeloperoxidase, and by catalase, which catalyzes the breakdown of hydrogen peroxide. Azides 101-106 myeloperoxidase Homo sapiens 0-15 1319066-3 1992 The viricidal activity of stimulated monocytes was inhibited by the peroxidase inhibitor azide, implicating MPO, and by catalase but not heated catalase or superoxide dismutase, implicating H2O2. Azides 89-94 myeloperoxidase Homo sapiens 108-111 1319066-5 1992 The viricidal activity of stimulated, glucose oxidase-supplemented CGD monocytes and MPO-supplemented MPO-deficient monocytes, like that of normal stimulated monocytes, was inhibited by azide and catalase. Azides 186-191 myeloperoxidase Homo sapiens 85-88 1319066-5 1992 The viricidal activity of stimulated, glucose oxidase-supplemented CGD monocytes and MPO-supplemented MPO-deficient monocytes, like that of normal stimulated monocytes, was inhibited by azide and catalase. Azides 186-191 myeloperoxidase Homo sapiens 102-105 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. Azides 238-243 myeloperoxidase Homo sapiens 25-40 1424279-6 1992 Addition of inhibitors to the chemiluminescence system demonstrated that the chemiluminescence response was inhibited by azide and salicylhydroxamic acid and reduced by histidine, suggesting that the chemiluminescence response was due to activation of myeloperoxidase, with generation of singlet oxygen. Azides 121-126 myeloperoxidase Homo sapiens 252-267 1352211-5 1992 Myeloperoxidase is likely the enzyme in the leukocyte involved, since the oxidation was inhibited by azide, which inhibits myeloperoxidase, and by catalase, which catalyzes the breakdown of hydrogen peroxide. Azides 101-106 myeloperoxidase Homo sapiens 123-138 1648459-3 1991 Since interaction between the cells and ionomycin was not associated with any notable superoxide production and hydrogen peroxide was induced only in the presence of azide, a potent inhibitor of the hydrogen peroxide-consuming enzymes catalase and myeloperoxidase, we conclude that this stimulus can generate oxygen metabolites intracellularly. Azides 166-171 myeloperoxidase Homo sapiens 248-263 1311041-10 1992 Azide, an inhibitor of MPO, and catalase, a scavenger of H2O2, inhibited the lytic activity of this system. Azides 0-5 myeloperoxidase Homo sapiens 23-26 1851410-3 1991 Over 95% of the luminol dependent chemiluminescence activated by all samples was inhibited by azide (indicating its dependence upon myeloperoxidase), but anti-(myeloperoxidase) IgG (which specifically inhibits only the extracellular activity of this enzyme) only inhibited the response stimulated by some samples: those fluids which activated the highest luminol dependent chemiluminescence also stimulated the greatest activity of an extracellular myeloperoxidase-H2O2 system. Azides 94-99 myeloperoxidase Homo sapiens 132-147 1654772-2 1991 Since luminol chemiluminescence (LCL) in neutrophils can be blocked by azide, an inhibitor of myeloperoxidase, LCL has been believed to reflect mainly the myeloperoxidase-catalyzed reaction. Azides 71-76 myeloperoxidase Homo sapiens 94-109 1654772-2 1991 Since luminol chemiluminescence (LCL) in neutrophils can be blocked by azide, an inhibitor of myeloperoxidase, LCL has been believed to reflect mainly the myeloperoxidase-catalyzed reaction. Azides 71-76 myeloperoxidase Homo sapiens 155-170 1849053-6 1991 Addition of azide, an MPO inhibitor, resulted in decreased tetraols from B[a]P-7,8-diol by PMNs or the MPO system. Azides 12-17 myeloperoxidase Homo sapiens 22-25 1849053-6 1991 Addition of azide, an MPO inhibitor, resulted in decreased tetraols from B[a]P-7,8-diol by PMNs or the MPO system. Azides 12-17 myeloperoxidase Homo sapiens 103-106 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. Azides 71-76 myeloperoxidase Homo sapiens 30-45 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). Azides 126-131 myeloperoxidase Homo sapiens 38-53 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). Azides 126-131 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). Azides 126-131 myeloperoxidase Homo sapiens 98-101 2169299-5 1990 The luminol response was inhibited by superoxide dismutase (SOD), catalase, and the MPO-inhibitor azide, while the lucigenin response was inhibited by SOD and catalase but stimulated by azide. Azides 98-103 myeloperoxidase Homo sapiens 84-87 2165113-3 1990 Further, both azide and catalase + superoxide dismutase inhibited the ability of normal neutrophils to damage hyphae, suggesting that this damage is mediated by products of the respiratory burst and by the MPO-halide system. Azides 14-19 myeloperoxidase Homo sapiens 206-209 2343183-5 1990 The addition of azide, CuDIPS, or taurine markedly inhibited the induction of SCEs by the combination of BP-7,8-diol and stimulated PMNs, further suggesting the involvement of myeloperoxidase in the activation of the polycyclic aromatic hydrocarbon. Azides 16-21 myeloperoxidase Homo sapiens 176-191 2157502-2 1990 However, since ionomycin and FMLP activity differ in their requirement for azide, a potent inhibitor of the hydrogen peroxide consuming enzymes catalase and myeloperoxidase, we propose that the two stimuli can activate different pools of the oxidase. Azides 75-80 myeloperoxidase Homo sapiens 157-172 2557840-10 1989 Inhibition of MPO by azide increased the magnitude, but not the duration, of .OH formation. Azides 21-26 myeloperoxidase Homo sapiens 14-17 2554813-10 1989 Addition of the MPO inhibitor azide to the reaction mixture had no effecting on resulting DMPO-OH or DMPO-CH3 peak amplitudes but increased that of DMPO-OOH. Azides 30-35 myeloperoxidase Homo sapiens 16-19 2542309-5 1989 Both loss of iron binding capacity and transferrin iodination by either the myeloperoxidase system or activated neutrophils were blocked by azide or catalase. Azides 140-145 myeloperoxidase Homo sapiens 76-91 2543723-2 1989 However, the presence of azide, a potent inhibitor of the hydrogen peroxide-consuming enzymes catalase and myeloperoxidase, was required to detect any release of hydrogen peroxide induced by ionomycin. Azides 25-30 myeloperoxidase Homo sapiens 107-122 2799756-3 1989 In ancillary experiments, the CL response of PMNs was inhibited by catalase (H2O2-scavenger), -azide (myeloperoxidase-MPO-inhibitor), taurine (hypochlorous acid-HOCl-scavenger) and chloride ion omission. Azides 95-100 myeloperoxidase Homo sapiens 102-117 2485131-7 1988 Studies on the possible role of the granulocyte enzyme myeloperoxidase in the activation and binding of these arylamines were conducted in vitro and also through the use of azide, an inhibitor of myeloperoxidase activity in cells. Azides 173-178 myeloperoxidase Homo sapiens 55-70 2540257-3 1989 Azide, a myeloperoxidase (MPO) inhibitor, reduced the CL reaction by more than 80%, which indicates that the CL reaction is dependent on the granule enzyme MPO. Azides 0-5 myeloperoxidase Homo sapiens 9-24 2540257-3 1989 Azide, a myeloperoxidase (MPO) inhibitor, reduced the CL reaction by more than 80%, which indicates that the CL reaction is dependent on the granule enzyme MPO. Azides 0-5 myeloperoxidase Homo sapiens 26-29 2540257-3 1989 Azide, a myeloperoxidase (MPO) inhibitor, reduced the CL reaction by more than 80%, which indicates that the CL reaction is dependent on the granule enzyme MPO. Azides 0-5 myeloperoxidase Homo sapiens 156-159 2535783-5 1989 However, in the presence of azide, a potent inhibitor of the hydrogen peroxide-consuming enzymes, catalase and myeloperoxidase, a pronounced release of hydrogen peroxide was also induced by ionomycin. Azides 28-33 myeloperoxidase Homo sapiens 111-126 2485131-7 1988 Studies on the possible role of the granulocyte enzyme myeloperoxidase in the activation and binding of these arylamines were conducted in vitro and also through the use of azide, an inhibitor of myeloperoxidase activity in cells. Azides 173-178 myeloperoxidase Homo sapiens 196-211 3038442-2 1987 Catalase, azide, cyanide and three aminoacids employed as quenchers of ClO, significantly inhibited this nonspecific cytotoxicity (NSC), suggesting an important role for the myeloperoxidase (MPO) system. Azides 10-15 myeloperoxidase Homo sapiens 174-189 2822016-3 1987 This was inhibited by azide and methionine, indicating that inactivation was due to myeloperoxidase-derived oxidants. Azides 22-27 myeloperoxidase Homo sapiens 84-99 3032797-9 1987 Azide inhibited the effects of the MPO-H2O2-Cl- system. Azides 0-5 myeloperoxidase Homo sapiens 35-38 6300255-2 1983 Inhibition by anaerobiosis, azide, cyanide, halide-free conditions, catalase, histidine, and tryptophan suggested mediation of hyphal damage primarily through the myeloperoxidase system. Azides 28-33 myeloperoxidase Homo sapiens 163-178 3016275-1 1986 The lysis of human red blood cells (HRBC) by neutrophil polymorphonuclear leukocytes (PMN), triggered with opsonized zymosan (OPZ) particles, was inhibited by azide, catalase, Cl- -free medium and amino acids indicating the involvement of myeloperoxidase (MPO), hydrogen peroxide (H2O2), Cl- ions and hypochlorous acid (HOCl) respectively. Azides 159-164 myeloperoxidase Homo sapiens 239-254 3016275-1 1986 The lysis of human red blood cells (HRBC) by neutrophil polymorphonuclear leukocytes (PMN), triggered with opsonized zymosan (OPZ) particles, was inhibited by azide, catalase, Cl- -free medium and amino acids indicating the involvement of myeloperoxidase (MPO), hydrogen peroxide (H2O2), Cl- ions and hypochlorous acid (HOCl) respectively. Azides 159-164 myeloperoxidase Homo sapiens 256-259 2989289-8 1985 Glutathione-glutathione peroxidase (GSH-GSH peroxidase), an extracellular H2O2 scavenger, totally protected neutrophil myeloperoxidase from inactivation by azide plus glucose-glucose oxidase. Azides 156-161 myeloperoxidase Homo sapiens 119-134 2989289-9 1985 In addition, when a mixture of normal and CGD cells was stimulated with PMA in the presence of azide, 90% of the myeloperoxidase in CGD neutrophils was inactivated. Azides 95-100 myeloperoxidase Homo sapiens 113-128 2989289-11 1985 In contrast, myeloperoxidase in normal polymorphonuclear leukocytes stimulated with PMA in the presence of azide and GSH-GSH peroxidase was 75% inactivated. Azides 107-112 myeloperoxidase Homo sapiens 13-28 4036175-5 1985 SubMIC penicillin pretreatment of S. pneumoniae R36A specifically promoted the susceptibility of these organisms to killing by myeloperoxidase (MPO)-mediated mechanisms (enhancement lost using MPO-deficient or azide-treated cells). Azides 210-215 myeloperoxidase Homo sapiens 127-142 4036175-5 1985 SubMIC penicillin pretreatment of S. pneumoniae R36A specifically promoted the susceptibility of these organisms to killing by myeloperoxidase (MPO)-mediated mechanisms (enhancement lost using MPO-deficient or azide-treated cells). Azides 210-215 myeloperoxidase Homo sapiens 144-147 6325409-6 1984 Fluorescent changes accompanying phagocytosis of serum-opsonized 5-isothiocyanatofluorescein-zymosan were also consistent with chlorination of the label; the changes were shown to be myeloperoxidase-dependent by use of myeloperoxidase-deficient or azide-treated cells. Azides 248-253 myeloperoxidase Homo sapiens 183-198 6295926-2 1983 The target cell lysis was prevented by azide, suggesting the involvement of the myeloperoxidase enzyme. Azides 39-44 myeloperoxidase Homo sapiens 80-95 3011897-3 1986 Detoxification required each component of the myeloperoxidase system and was prevented by the addition of agents that inhibit heme enzymes (azide, cyanide) or degrade H2O2 (catalase). Azides 140-145 myeloperoxidase Homo sapiens 46-61 2991910-2 1985 Cu(II)(3,5-diisopropylsalicylic acid)2 (CuDIPS), a biomimetic superoxide dismutase, and azide, a myeloperoxidase inhibitor, inhibited both of these reactions, indicating a dependency on oxygen-derived oxidants in these hydrocarbon-activation processes. Azides 88-93 myeloperoxidase Homo sapiens 97-112 2989289-1 1985 Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide. Azides 79-84 myeloperoxidase Homo sapiens 38-53 2989289-3 1985 In this report, we show that myeloperoxidase is also inactivated by H2O2 plus azide. Azides 78-83 myeloperoxidase Homo sapiens 29-44 2989289-5 1985 Stimulation of neutrophils with phorbol myristate acetate (PMA, 100 ng/ml) plus azide (5 mM) for 30 min completely inactivated intragranular myeloperoxidase and reduced cytosolic catalase to 35% of resting cells. Azides 80-85 myeloperoxidase Homo sapiens 141-156 2989289-7 1985 Incubation of neutrophils with azide and a H2O2 generating system (glucose-glucose oxidase) inactivated 41% of neutrophil myeloperoxidase. Azides 31-36 myeloperoxidase Homo sapiens 122-137 6318832-8 1984 EPR spectroscopy of low-spin cyanide and azide derivatives of eosinophil peroxidase, lactoperoxidase, myeloperoxidase and catalase revealed that the haem-ligand structure of eosinophil peroxidase is closely related to lactoperoxidase, whereas that of myeloperoxidase shows great resemblance to catalase. Azides 41-46 myeloperoxidase Homo sapiens 102-117 6292103-9 1982 Damage to hyphae by the myeloperoxidase system was inhibited by azide, cyanide, catalase, histidine, and tryptophan, but not by superoxide dismutase, dimethyl sulfoxide, or mannitol. Azides 64-69 myeloperoxidase Homo sapiens 24-39 6277912-3 1982 The addition of catalase or the myeloperoxidase inhibitor, azide, protected all three prostaglandins from the phorbol-stimulated neutrophils. Azides 59-64 myeloperoxidase Homo sapiens 32-47 6271809-10 1981 This conclusion was based on the kinetics and dose-response relationships for the effects of azide and cyanide on H2O2 release and on the activities of catalase and myeloperoxidase. Azides 93-98 myeloperoxidase Homo sapiens 165-180 6252248-5 1980 Azide, which in addition to its blocking action on oxydative phosphorylation also inhibits catalase and myeloperoxidase, resulted in a approximately equal to 40% stimulation of ADCC by cells from normals but was without effect of ADCC by cells from CGD patients. Azides 0-5 myeloperoxidase Homo sapiens 104-119 6162845-3 1981 Inactivation was rapid (10 to 20 s); required active myeloperoxidase, micromolar concentrations of H2O2 (or glucose oxidase as a peroxide generator), and a halide cofactor (Cl- or I-); and was blocked by azide, cyanide, and catalase. Azides 204-209 myeloperoxidase Homo sapiens 53-68 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. Azides 199-204 myeloperoxidase Homo sapiens 87-102 6267057-5 1981 In a cell-free system, the fluorescence of 3,3"-dipropylthiodicarbocyanine, but not that of 3,3"-dipentyloxadicarbocyanine, was rapidly eliminated by myeloperoxidase in the presence of hydrogen peroxide and a halide; this loss of fluorescence was inhibited by azide, cyanide, or catalase. Azides 260-265 myeloperoxidase Homo sapiens 150-165 180060-5 1976 Light emission by normal leukocytes is strongly inhibited by both superoxide dismutase and azide, whereas that of myeloperoxidase-deficient leukocytes, while still strongly inhibited by superoxide dismutase is considerably less sensitive to azide. Azides 242-247 myeloperoxidase Homo sapiens 114-129 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 33-38 myeloperoxidase Homo sapiens 16-19 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 33-38 myeloperoxidase Homo sapiens 163-166 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 103-108 myeloperoxidase Homo sapiens 16-19 212502-6 1978 The presence of MPO-independent, azide-stimulable systems in the PMN preparations was suggested by the azide stimulation of ethylene formation from methional when MPO-deficient leukocytes were employed. Azides 103-108 myeloperoxidase Homo sapiens 163-166 6244848-2 1980 The reaction of myeloperoxidase with fluoride, chloride and azide has been studied by EPR. Azides 60-65 myeloperoxidase Homo sapiens 16-31 180060-7 1976 Light emission by the xanthine oxidase model system is strongly inhibited by superoxide dismutase and is not inhibited by azide, whereas the myeloperoxidase-dependent model system is strongly inhibited by azide but only slightly inhibited by superoxide dismutase. Azides 205-210 myeloperoxidase Homo sapiens 141-156 170101-6 1975 Chlorination in neutrophils is inhibited by the iodide and myeloperoxidase inhibitors azide and cyanide. Azides 86-91 myeloperoxidase Homo sapiens 59-74 5116211-3 1971 Azide and cyanide increased glucose C-1 oxidation by normal leukocytes but had little or no effect on myeloperoxidase-deficient leukocytes suggesting that these agents normally stimulate glucose C-1 oxidation, in part, by inhibition of myeloperoxidase. Azides 0-5 myeloperoxidase Homo sapiens 236-251 4988715-1 1970 Azide and, to a lesser extent, cyanide inhibit the microbicidal activity of myeloperoxidase and of intact normal leukocytes, but they have little or no effect on peroxidase-negative leukocytes. Azides 0-5 myeloperoxidase Homo sapiens 76-91