- Venge P, Dahl R. The eosinophil and intrinsic asthma. Agents Actions 1989; 28: 67–74.
- Gleich GJ, Ottesen EA, Leiferman KM, Ackerman SJ. Eosinophils and human disease. Int Arch Allergy Appl Immunol 1989; 88: 59–62.
- Barnes PJ, Chung KF, Page CP. Inflammatory mediators of asthma: an update. Pharmacol Rev 1998; 50: 515–596.
- Wardlaw AJ. Eosinophils in the 1990s: new perspectives on their role in health and disease. Postgrad Med J 1994; 70: 536–552.
- Horwitz RJ, Busse WW. Inflammation and asthma. Clin Chest Med 1995; 16: 583–602.
- Rothenburg ME. Eosinophilia. N Engl J Med 1998; 338: 1592–1600.
- Holgate ST. The epidemic of allergy and asthma. Nature 1999; 402 ( Suppl.): B2-B4.
- Ehrlich P. Ueber die specifischen granulationen des Blutes. Arch Arzat Physiol Lp 3 Physiol Abt 1879; 571-579.
- Gollasch. Zurkenntnis des asthatischen sputums. Fortschr Med 1889; 7: 28.
- Hamann KJ, Barker RL, Ten RM, Gleich GJ. The molecular biology of eosinophil granule proteins. Int Arch Allergy Appl Immunol 1991; 94: 202–209.
- Monteseirin J, Prados M, Bonilla let al. Granular proteins of eosinophils. Allergol Immunopathol 1996; 24: 219–225.
- Allen JN, Davis WB, Pacht ER. Diagnostic significance of increased bronchoalveolar lavage fluid eosinophils. Am Rev Respir Dis 1990; 142: 642–647.
- Griffin E, Hakansson L, Formgren H, Jorgensen K, Peterson C, Venge P. Blood eosinophil number and activity in relation to lung function in patients with asthma and with eosinophilia. J Allergy Clin Immunol 1991; 87: 548–557.
- Sanz ML, Parra A, Prieto I, Dieguez I, Oehling AK. Serum eosinophil peroxidase (EPO) levels in asthmatic patients. Allergy 1997; 52: 417–422.
- Brottman GM, Regelmann WE, Slungaard A, Wangensteen OD. Effect of eosinophil peroxidase on airway epithelial permeability in the guinea pig. Pediatr Pulmonol 1996; 21: 159–166.
- Yoshikawa S, Kayes SG, Parker JC. Eosinophils increase lung microvascular permeability via the peroxidase-hydrogen peroxide-halide system. Bronchoconstriction and vasoconstriction unaffected by eosinophil peroxidase inhibition. Am Rev Respir Dis 1993; 147: 914–920.
- Pretolani M, Ruffle C, Joseph D et al. Role of eosinophil activation in the bronchial reactivity of allergic guinea pigs. Am J Respir Crit Care Med 1994; 149: 1167–1174.
- Hamann KJ, Strek ME, Baranowski SL et al. Effects of activated eosinophils cultured from human umbilical cord blood on guinea pig trachealis. Am J Physiol 1993; 265: L301–L307.
- Minnicozzi M, Duran WN, Gleich GJ, Egan RW. Eosinophil granule proteins increase microvascular macromolecular transport in the hamster cheek pouch. J Immunol 1994; 153: 2664–2670.
- Gundel RH, Letts LG, Gleich GJ. Human eosinophil major basic protein induces airway constriction and airway hyperresponsiveness in primates. J Clin Invest 1991; 87: 1470–1473.
- Dalde'n SE, Hedquist P, Hammarstrom S, Sammelsson B. Leukotrienes are potent constrictors of human bronchi. Nature 1980; 288: 484–486.
- Shaw RJ, Cromwell 0, Kay AB. Preferential generation of leukotriene C4 by human eosinophils. Clin Exp Immunol 1984; 56: 716.
- Shaw RJ, Walsh GM, Cromwell 0, Moqbel R, Spry CJF, Kay AB. Activated human eosinophils generate SRS-A leukotrienes following physiological (IgG dependent) stimulation. Nature 1985; 316: 150–152.
- Bruijnzeel PL. Contribution of eosinophil-derived mediators in asthma. Int Arch Allergy Appl Immunol 1989; 90 (Suppl. 1): 57-63.
- Kazura JW, Fanning MM, Blumer JL, Mahmoud AA. Role of cell-generated hydrogen peroxide in granulocyte-mediated killing of schistosomula of Schistosoma mansoni in vitro. J Clin Invest 1981; 67: 93–102.
- Klebanoff SJ, Locksley RM, Jong EC, Rosen H. Oxidative response of phagocytes to parasite invasion. Ciba Found Symp 1983; 99: 92–112.
- Babior BM, Kipnes RS, Curnutte JT. Biological defense mechanism: the production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest 1973; 52: 741–744.
- Jong EC, Henderson WR, Klebanoff SJ. Bactericidal activity of eosinophil peroxidase. J Immunol 1980; 124: 1378–1382.
- Segal BH, Leto TL, Gallin JI, Malech HL, Holland SM. Genetic, biochemical, and clinical features of chronic granulomatous disease. Medicine (Baltimore) 2000; 79: 170–200.
- DeChatelet LR, Shirley PS, McPhail LC, Huntley CC, Muss HB, Bass DA. Oxidative metabolism of the human eosinophil. Blood 1977; 50: 525–535.
- Slungaard A, Vercellotti GM, Walker G, Nelson RD, Jacob HS. Tumor necrosis factor alpha/cachectin stimulates eosinophil oxidant production and toxicity towards human endothelium. J Exp Med 1990; 171: 2025–2041.
- Someya A, Nishijima K, Nunoi H, Irie S, Nagaoka I. Study on the superoxide-producing enzyme of eosinophils and neutrophils - comparison of the NADPH oxidase components. Arch Biochem Biophys 1997; 345: 207–213.
- Merlie JP, Fagan D, Mudd J, Needleman P. Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase). J Biol Chem 1988; 263: 3550–3553.
- Kimura S, Ikeda-Saito M. Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionarily related members of the same gene family. Proteins Struct Funct Genet 1988; 3: 113–120.
- Cals MM, Maillart P, Brignon G, Anglade P, Dumas BR. Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family. Eur J Biochem 1991; 198: 733–739.
- Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ. Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxide superfamily. J Exp Med 1989; 169: 1757–1769.
- Podrez EA, Abu-Soud HM, Hazen SL. Myeloperoxidase-generated oxidants and atherosclerosis. Free Radic Biol Med 2000; In press.
- Jong EC, Klebanoff SJ. Eosinophil-mediated mammalian tumor cell cytotoxicity: role of the peroxidase system. J Immunol 1980; 124: 1949–1953.
- Agosti JM, Altman LC, Ayars Gil, Loegering DA, Gleich GJ, Klebanoff SJ. The injurious effect of eosinophil peroxidase, hydrogen peroxide, and halides on pneumocytes in vitro. J Allergy Clin Immunol 1987; 79: 496–504.
- Ayars Gil, Altman LC, McManus MM et al. Injurious effect of the eosinophil peroxidase-hydrogen peroxide-halide system and major basic protein on human nasal epithelium in vitro. Am Rev Respir Dis 1989; 140: 125–131.
- Slungaard A, Mahoney JR Jr. Bromide-dependent toxicity of eosinophil peroxidase for endothelium and isolated working rat hearts: a model for eosinophilic endocarditis. J Exp Med 1991; 173: 117–126.
- Samoszuk MK, Nguyen V, Thomas C, Jacobson D. Effects of sonicated eosinophils on the in vivo sensitivity of human lymphoma cells to glucose oxidase. Cancer Res 1994; 54: 2650–2653.
- Anni H, Yonetani T. Mechanism of action of peroxidases. Met Ions Biol Syst 1992; 28: 219–241.
- Dunford HB. Peroxidases. Adv Inorg Biochem 1982; 4: 41–68.
- Finzel BC, Poulos TS, Kraut J. Crystal structure of yeast cytochrome c peroxidase refined at 1.7 A resolution. J Biol Chem 1984; 259: 13027–13036.
- Dawson JH. Probing structure-function relations in heme-containing oxygenases and peroxidases. Science 1988; 240: 433–439.
- Monzani E, Gatti AL, Profumo A, Casella L, Gullotti M. Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover. Biochemistry 1997; 36: 1918–1926.
- Courtin F, Deme D, Virion A, Michot J-L, Pommier J, Nunez J. The role of lactoperoxidase-I1202 compounds in the catalysis of thyroglobulin iodination and thyroid hormone synthesis. Eur J Biochem 1982; 124: 603–609.
- Courtin F, Michot J-L, Virion A, Pommier J, Deme D. Reduction of lactoperoxidase-H202 compounds by ferrocyanide: indirect evidence of an apoprotein site for one of the two oxidizing equivalents. Biochem Biophys Res Commun 1984; 121: 463–470.
- Hori H, Fenna RE, Kimura S, Ikeda-Saito M. Aromatic substrate molecules bind at the distal heme pocket of myeloperoxidase. J Biol Chem 1994; 269: 8388–8392.
- Fiedler TJ, Davey CA, Fenna RE. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem 2000; 275: 11964–11971.
- Slungaard A, Mahoney JR Jr. Thiocyanate is the major substrate for eosinophil peroxidase in physiologic fluids. Implications for cytotoxicity. J Biol Chem 1991; 266: 4903–4910.
- Weiss SJ, Test ST, Eckmann CM, Ross D, Regiania S. Brominating oxidants generated by human eosinophils. Science 1986; 234: 200–203.
- Mayeno AN, Curran AJ, Roberts RL, Foote CS. Eosinophils preferentially use bromide to generate halogenating agents. J Biol Chem 1989; 264: 5660–5668.
- Wu W, Samoszuk MK, Comhair SAA et al. Eosinophils generate brominating oxidants in allergen-induced asthma. J Clin Invest 2000; 105: 1455–1463.
- van Dalen CJ, Whitehouse MW, Winterbourn CC, Kettle AJ. Thiocyanate and chloride as competing substrates for myeloperoxidase. Biochem J 1997; 327: 487–492.
- Abu-Soud HM, Hazen SL. Nitric oxide is a physiological substrate for mammalian peroxidases. In review.
- Thomas EL, Bozeman PM, Jefferson MM, King CC. Oxidation of bromide by the human leukocyte enzymes myeloperoxidase and eosinophil peroxidase. Formation of bromoamines. J Biol Chem 1995; 270: 2906–2913.
- Linder M. Nutritional Biochemistry and Metabolism. New York, NY: Elsevier, 1992; 98.
- Teitz NW. Drugs: therapeutic and toxic. In: Burris CA, Ashwood ER. (eds) Teitz Textbook of Clinical Chemistry. Philadelphia, PA: Saunders, 1999; 1097.
- Hazen SL, Hsu FF, Mueller DM, Crowley JR, Heinecke JW. Human neutrophils employ chlorine gas as an oxidant during phagocytosis. J Clin Invest 1996; 98: 1283–1289.
- Hazen SL, Crowley JR, Mueller DM, Heinecke JW. Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation. Free Radic Biol Med 1997; 23: 909–916.
- Hazen SL, Heinecke JW. 3-Chlorotyrosine, a specific marker of myeloperoxidase-catalyzed oxidation, is markedly elevated in low density lipoprotein isolated from human atherosclerotic J Clin Invest 1997; 99: 2075-2081.
- Kettle AJ. Neutrophils convert tyrosyl residues in albumin to chlorotyrosine. FEBS Lett 1996; 379: 103–106.
- Wu W, Chen Y, d'Avignon A, Hazen SL. 3-Bromotyrosine and 3,5-dibromotyrosine are major products of protein oxidation by eosinophil peroxidase: potential markers for eosinophil-dependent tissue injury in vivo. Biochemistry 1999; 38: 3538-3548.
- Domigan NM, Charlton TS, Duncan MW, Winterbourn CC, Kettle AJ. Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils. J Biol Chem 1995; 270: 16542–16548.
- Albrich JM, McCarthy CA, Hurst JK. Biological reactivity of hypochlorous acid: implications for microbicidal mechanisms of leukocyte myeloperoxidase. Proc Natl Acad Sci USA 1981; 78: 210–214.
- Harrison JE, Schultz J. Studies on the chlorinating activity of myeloperoxidase. J Biol Chem 1976; 251: 1371–1374.
- Hazen SL, Gaut JP, Hsu FF, Crowley JR, d'Avignon A, Heinecke JW. p-Hydroxyphenylacetaldehyde, the major product of L-tyrosine oxidation by the myeloperoxidase-I1202-chloride system of phagocytes, covalently modifies epsilon-amino groups of protein lysine residues. J Biol Chem 1997; 272: 16990–16998.
- Hazen SL, Crowley JR, Mueller DM, Heinecke JW. Mass spectrometric quantification of 3-chlorotyrosine in human tissues with attomole sensitivity: a sensitive and specific marker for myeloperoxidase-catalyzed chlorination at sites of inflammation. Free Radic Biol Med 1997; 23: 909–916.
- Kettle AJ, Winterbourn CC. Assays for the chlorination activity of myeloperoxidase. Methods Enzymol 1994; 233: 502–512.
- Grisham MB, Jefferson MM, Melton DF, Thomas EL. Chlorination of endogenous amines by isolated neutrophils. Ammonia-dependent bactericidal, cytotoxic, and cytolytic activities of the chloramines. J Biol Chem 1984; 259: 10404–10413.
- Marquez LA, Dunford HB. Chlorination of taurine by myeloperoxidase. Kinetic evidence for an enzyme-bound intermediate. J Biol Chem 1994; 269: 7950–7956.
- Wajon JE, Morris JC. Bromination chemistry: rates of formation of NH2Br and some N-brominated amino acids. In: Jolley RL, Brungs WA, Cumming RB, Jacobs VA. (eds) Water Chlorination: Environmental Impact and Health Effects, vol. 3. Ann Arbor, MI: Ann Arbor Science, 1980; 171-181.
- Kanofsky JR. Bromine derivatives of amino acids as intermediates in the peroxidase-catalyzed formation of singlet oxygen. Arch Biochem Biophys 1989; 274: 229–234.
- Kanofsky JR, Hoogland H, Weyer R, Weiss SJ. Singlet oxygen production by human eosinophils. J Biol Chem 1988; 263: 9692–9696.
- Hazen SL, d'Avignon A, Anderson MM, Hsu FF, Heinecke JW. Human neutrophils employ the myeloperoxidase-hydrogen peroxide-chloride system to oxidize alpha-amino acids to a family of reactive aldehydes. Mechanistic studies identifying labile intermediates along the reaction pathway. J Biol Chem 1998; 273: 4997–5005.
- Hazen SL, Hsu FF, d'Avignon A, Heinecke JW. Human neutrophils employ myeloperoxidase to convert a-amino acids to a battery of reactive aldehydes: a pathway for aldehyde formation at sites of inflammation. Biochemistry 1998; 37: 6864–6873.
- Wajon JE, Morris JC. Rates of formation of N-bromo amines in aqueous solution. Inorg Chem 1982; 21: 4258–4263.
- Hazen SL, Hsu FF, Heinecke JW. p-Hydroxyphenylacetaldehyde is the major product of L-tyrosine oxidation by activated human phagocytes: a chloride-dependent mechanism for the conversion of free amino acids into reactive aldehydes by myeloperoxidase. J Biol Chem 1996; 271: 1861–1867.
- de la Mare PBD, Ridd JH. Aromatic Substitution: Nitration and Halogenation. London: Butterworth, 1959; 105–129.
- MacPherson JC, Comhair SA, Erzurum SC et al. Eosinophils are a major source of NO-derived oxidants in severe asthma: characterization of pathways available to eosinophils for generating reactive nitrogen species. In review.
- Carr AC, van den Berg JJ, Winterbourn CC. Differential reactivities of hypochlorous and hypobromous acids with purified Escherichia coli phospholipid: formation of haloamines and halohydrins. Biochim Biophys Acta 1998; 1392: 254–264.
- Shen A, Mitra SN, Wu W et al. Eosinophil peroxidase brominates free nucleotides and double stranded DNA: identification of novel markers for oxidative damage. In review.
- Hazen SL, Hsu FF, Duffin K, Heinecke JW. Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols. J Biol Chem 1996; 271: 23080–23088.
- Hazen SL, Hsu FF, Gaut JP, Crowley JR, Heinecke JW. Modification of proteins and lipids by myeloperoxidase. Methods Enzymol 1999; 300: 88–105.
- Henderson JP, Byun J, Heinecke JW. Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes produces 5-chlorocytosine in bacterial RNA. J Biol Chem 1999; 274: 33440–33448.
- Ramos CL, Pou S, Britigan BE, Cohen MS, Rosen GM. Spin trapping evidence for myeloperoxidase-dependent hydroxyl radical formation by human neutrophils and monocytes. J Biol Chem 1992; 267: 8307–8312.
- McCormick ML, Roeder TL, Railsback MA, Britigan BE. Eosinophil peroxidase-dependent hydroxyl radical generation by human eosinophils. J Biol Chem 1994; 269: 27914–27919.
- Subrahmanyam VV, Kolachana P, Smith MT. Hydroxylation of phenol to hydroquinone catalyzed by a human myeloperoxidase-superoxide complex: possible implications in benzene-induced myelotoxicity. Free Radic Res Commun 1991; 15: 285–296.
- Candeias LP, Patel KB, Stratford MR, Wardman P. Free hydroxyl radicals are formed on reaction between the neutrophil-derived species superoxide anion and hypochlorous acid. FEBS Lett 1993; 333: 151–153.
- Long CA, Bielski BHT. Rate of reaction of superoxide radical with chloride-containing species. J Phys Chem 1980; 84: 555–557.
- Ross AB, Mallard NG, Helman WP, Bielski BHT, Buxton GV. NDRL-NIST Solution Kinetics Database, ver. 1.1999.
- Shen Z, Wu W, Hazen SL. Activated leukocytes oxidatively damage DNA, RNA and the nucleotide pool through halide-dependent formation of hydroxyl radical. Biochemistry 2000; 39: 5474–5482.
- Kaplan RP. Cancer complicating chronic ulcerative and scarifying mucocutaneous disorders. Adv Dennatol 1987; 2: 19–46.
- Gordon LI, Weitzman SA. The respiratory burst and carcinogenesis. In: Sbarra AJ, Strauss RR. (eds) The Respiratory Burst and its Physiological Significance. New York, NY: Plenum, 1988; 277–298.
- Preston-Martin S, Pike MC, Ross RIC, Jones PA, Henderson BE. Increased cell division as a cause of human cancer. Cancer Res 1991; 50: 7415–7421.
- Rosin MP, Anwar WA, Ward AJ. Inflammation, chromosomal instability, and cancer: the schistosomiasis model. Cancer Res 1994; 54: 1929s-1933s.
- Sithithaworn P, Haswell-Elkins MR, Mairiang P et al. Parasite-associated morbidity: liver fluke infection and bile duct cancer in north-east Thailand. Int J Parasitol 1994; 24: 833–843.
- Haswell-Elkins MR, Satarug S, Tsuda M et al. Liver fluke infection and cholangiocarcinoma: model of endogenous nitric oxide and extragastric nitrosation in human carcinogenesis. Mutat Res 1994; 305: 241–252.
- Ishii A, Matsuoka H, Aji T et al. Parasite infection and cancer: with special emphasis on Schistosoma japonicum infections (Trematoda). Mutat Res 1994; 305: 273–281.
- Loft S, Poulsen HE. Cancer risk and oxidative DNA damage in man. J Mol Med 1996; 74: 297–312.
- Aune TM, Thomas EL, Morrison M. Lactoperoxidase-catalyzed incorporation of thiocyanate ion into a protein substrate. Biochemistry 1977; 16:4611.
- Thomas EL, Fishman M. Oxidation of chloride and thiocyanate by isolated leukocytes. J Biol Chem 1986; 261: 9694–9702.
- Thomas EL. Products of lactoperoxidase-catalysed oxidation of thiocyanate. In: Pruitt KM, Tenovou JO. (eds) The Lactoperoxidase System, Chemistry and Biological Significance. New York, NY: Marcel Dekker, 1985; 31–53.
- Modi S, Deodhar SS, Behere DV, Mitra S. Lactoperoxidase-catalyzed oxidation of thiocyanate by hydrogen peroxide: “N nuclear magnetic resonance and optical spectral studies. Biochemistry 1991; 30: 118–124.
- Pollock JR, Goff HM. Lactoperoxidase-catalyzed oxidation of thio-cyanate ion: a carbon-13 nuclear magnetic resonance study of the oxidation products. Biochim Biophys Acta 1992; 1159: 279–285.
- Lovaas E. Free radical generation and coupled thiol oxidation by lactoperoxidase/SCN/11202. Free Radic Biol Med 1992; 13: 187–195.
- Arlandson M, Decker T, Roongta VA et al. Eosinophil peroxidase oxidation of thiocyanate: characterization of major reaction products and a potential sulfhydryl-targeted cytotoxicity system. In review.
- Stark GR. Modification of proteins with cyanate. Methods Enzymol 1967; 11: 590–594.
- Barnes PJ. Nitric oxide and asthma. Res Immunol 1995; 146: 698–702.
- Sanders SP. Nitric oxide in asthma. Pathogenic, therapeutic, or diagnostic? Am J Respir Cell Mol Biol 1999; 21: 147–149.
- Ashutosh K. Nitric oxide and asthma: a review. Curr Opin Pulm Med 2000; 6: 21–25.
- Guo FH, Comhair SAA, Zheng S et al. Molecular mechanisms of increased nitric oxide (NO) in asthma: evidence for transcriptional and post-translational regulation of NO synthesis. J Immunol 2000; 164: 5970–5980.
- Wu W, Chen Y, Hazen SL. Eosinophil peroxidase nitrates protein tyrosyl residues: implications for oxidative damage by nitrating intermediates in eosinophilic inflammatory disorders. J Biol Chem 1999; 274: 25933–25944.
- van der Vliet A, Eiserich JP, Halliwell B, Cross CE. Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J Biol Chem 1997; 272: 7617–7625.
- Burner U, Furtmiiller PG, Kettle AJ, Koppenol WH, Obinger C. Mechanism of reaction of myeloperoxidase with nitrite. J Biol Chem 2000; 275: 20597–20601.
- Schmitt D, Shen Z, Mang R et al. Leukocytes utilize myeloperoxidase-generated nitrating intermediates as physiological catalysts for the generation of biologically active oxidized lipids and sterols in serum. Biochemistry 1999; 38: 16904–16915.
- Hazen SL, Mang R, Shen Z et al. Formation of nitric oxide-derived oxidants by myeloperoxidase in monocytes: pathways for monocyte-mediated protein nitration and lipid peroxidation in vivo. Circ Res 1999; 85: 950–958.
- Podrez EA, Schmitt D, Hoff HF, Hazen SL. Myeloperoxidase-generated reactive nitrogen species convert LDL into an atherogenic form in vitro. J Clin Invest 1999; 103: 1547-1560.
- Podrez EA, Febbraio M, Sheibani Net al. Macrophage scavenger receptor CD36 is the major receptor for LDL modified by monocyte-generated reactive nitrogen species. J Clin Invest 2000; 105: 1095–1108
- MacPherson J, Hazen SL. Eosinophil peroxidase generates bioactive eicosanoids via formation of reactive nitrogen species. Free Radic Biol Med 1999; 27 ( Suppl.): S95.
- Stelts D, Egan RW, Falcone A et al. Eosinophils retain their granule major basic protein in a murine model of allergic pulmonary inflammation. Am J Respir Cell Mol Biol 1998; 18: 463–470.
- Nauseef WM. Myeloperoxidase deficiency. Hematol Pathol 1990; 4: 165–178.
- Presentey B, Joshua H. Peroxidase and phospholipid deficiency in human eosinophil granulocytes — a marker in population genetics. Experientia 1982; 38: 628–629.
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Role of eosinophil peroxidase in the origins of protein oxidation in asthma
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