메뉴 건너뛰기




Volumn 298, Issue 12, 1978, Pages 659-668

Oxygen-Dependent Microbial Killing by Phagocytes

Author keywords

[No Author keywords available]

Indexed keywords

OXYGEN;

EID: 0017834531     PISSN: 00284793     EISSN: 15334406     Source Type: Journal    
DOI: 10.1056/NEJM197803232981205     Document Type: Review
Times cited : (1666)

References (100)
  • 1
    • 0004992889 scopus 로고
    • Untersuchungen über die intracellulare Verdauung bei wirbellosen Thieren
    • Metschnikoff E: Untersuchungen über die intracellulare Verdauung bei wirbellosen Thieren. Arb Zoologischen Inst Univ Wien 5: 141–168, 1883
    • (1883) Arb Zoologischen Inst Univ Wien , vol.5 , pp. 141-168
    • Metschnikoff, E.1
  • 2
    • 85023703013 scopus 로고
    • Selected Plays with Prefaces
    • Vol 1. New York, Dodd Mead
    • Shaw GB: Selected Plays with Prefaces. Vol 1. New York, Dodd Mead, 1957, p 110
    • (1957) , pp. 110
    • Shaw, G.B.1
  • 3
    • 0016443593 scopus 로고
    • Physiology of chemotaxis and random motility
    • Keller HU, Hess MW, Cottier H: Physiology of chemotaxis and random motility. Semin Hematol 12: 47–57, 1975
    • (1975) Semin Hematol , vol.12 , pp. 47-57
    • Keller, H.U.1    Hess, M.W.2    Cottier, H.3
  • 4
    • 0016316725 scopus 로고
    • Mechanisms of sensing chemical gradients by polymorphonuclear leukocytes
    • Zigmond SH: Mechanisms of sensing chemical gradients by polymorphonuclear leukocytes. Nature 249: 450–452, 1974
    • (1974) Nature , vol.249 , pp. 450-452
    • Zigmond, S.H.1
  • 5
    • 0016458579 scopus 로고
    • Phagocytosis: recognition and ingestion
    • Stossel TP: Phagocytosis: recognition and ingestion. Semin Hematol 12: 83–116, 1975
    • (1975) Semin Hematol , vol.12 , pp. 83-116
    • Stossel, T.P.1
  • 6
    • 0343351492 scopus 로고
    • Electron microscope studies on the degranulation of rabbit peritoneal leukocytes during phagocytosis
    • Zucker-Franklin D, Hirsch JG: Electron microscope studies on the degranulation of rabbit peritoneal leukocytes during phagocytosis. J Exp Med 120: 569–576, 1964
    • (1964) J Exp Med , vol.120 , pp. 569-576
    • Zucker-Franklin, D.1    Hirsch, J.G.2
  • 7
    • 0000054142 scopus 로고
    • The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes
    • Sbarra AJ, Karnovsky ML: The biochemical basis of phagocytosis. I. Metabolic changes during the ingestion of particles by polymorphonuclear leukocytes. J Biol Chem 234: 1355–1362, 1959
    • (1959) J Biol Chem , vol.234 , pp. 1355-1362
    • Sbarra, A.J.1    Karnovsky, M.L.2
  • 8
    • 0015139958 scopus 로고
    • The development of neutrophilic polymorphonuclear leukocytes in human bone marrow: origin and content of azurophil and specific granules
    • Bainton DF, Ullyot JL, Farquhar MG: The development of neutrophilic polymorphonuclear leukocytes in human bone marrow: origin and content of azurophil and specific granules. J Exp Med 134: 907–934, 1971
    • (1971) J Exp Med , vol.134 , pp. 907-934
    • Bainton, D.F.1    Ullyot, J.L.2    Farquhar, M.G.3
  • 9
    • 0016403710 scopus 로고
    • Phagocytosis
    • Stossel TP: Phagocytosis. N Engl J Med 290: 717–723, 774–780, 833–839, 1974
    • (1974) N Engl J Med , vol.290 , pp. 717-723
    • Stossel, T.P.1
  • 10
    • 0000792494 scopus 로고
    • The extra respiration of phagocytosis
    • Baldridge CW, Gerard RW: The extra respiration of phagocytosis. Am J Physiol 103: 235–236, 1933
    • (1933) Am J Physiol , vol.103 , pp. 235-236
    • Baldridge, C.W.1    Gerard, R.W.2
  • 11
    • 0014276965 scopus 로고
    • The metabolism of leukocytes
    • Karnovsky ML: The metabolism of leukocytes. Semin Hematol 5: 156–165, 1968
    • (1968) Semin Hematol , vol.5 , pp. 156-165
    • Karnovsky, M.L.1
  • 12
    • 0017332291 scopus 로고
    • 2
    • Simon LM, Robin ED, Phillips JR, et al: Enzymatic basis for bioenergetic differences of alveolar versus peritoneal macrophages and enzyme regulation by molecular O2. J Clin Invest 59: 443–448, 1977
    • (1977) J Clin Invest , vol.59 , pp. 443-448
    • Simon, L.M.1    Robin, E.D.2    Phillips, J.R.3
  • 13
    • 0345625634 scopus 로고
    • Metabolic patterns in three types of phagocytizing cells
    • Oren R, Farnham AE, Saito K, et al: Metabolic patterns in three types of phagocytizing cells. J Cell Biol 17: 487–501, 1963
    • (1963) J Cell Biol , vol.17 , pp. 487-501
    • Oren, R.1    Farnham, A.E.2    Saito, K.3
  • 14
    • 0015024660 scopus 로고
    • Metabolic and bactericidal activities of human eosinophils
    • Baehner RL, Johnston RB Jr: Metabolic and bactericidal activities of human eosinophils. Br J Haematol 20: 277–285, 1971
    • (1971) Br J Haematol , vol.20 , pp. 277-285
    • Baehner, R.L.1    Johnston, R.B.2
  • 15
    • 0000725406 scopus 로고
    • Biochemical aspects of phagocytosis
    • Iyer GYN, Islam MF, Quastel JH: Biochemical aspects of phagocytosis. Nature 192: 535–541, 1961
    • (1961) Nature , vol.192 , pp. 535-541
    • Iyer, G.1    Islam, M.F.2    Quastel, J.H.3
  • 16
    • 1542752111 scopus 로고
    • Occurrence and control of the phosphogluconate oxidation pathway in normal and leukemic leukocytes
    • Beck WS: Occurrence and control of the phosphogluconate oxidation pathway in normal and leukemic leukocytes. J Biol Chem 232: 271–283, 1958
    • (1958) J Biol Chem , vol.232 , pp. 271-283
    • Beck, W.S.1
  • 17
    • 0014691242 scopus 로고
    • Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein)
    • McCord JM, Fridovich I: Superoxide dismutase: an enzymic function for erythrocuprein (hemocuprein). J Biol Chem 244: 6049–6055, 1969
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 18
    • 0015596284 scopus 로고
    • Biological defense mechanisms: the production by leukocytes of superoxide, a potential bactericidal agent
    • Babior BM, Kipnes RS, Curnutte JT: Biological defense mechanisms: the production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest 52: 741–744, 1973
    • (1973) J Clin Invest , vol.52 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curnutte, J.T.3
  • 19
    • 0016427825 scopus 로고
    • Superoxide production by phagocytic leukocytes
    • Drath DB, Karnovsky ML: Superoxide production by phagocytic leukocytes. J Exp Med 141: 257–262, 1975
    • (1975) J Exp Med , vol.141 , pp. 257-262
    • Drath, D.B.1    Karnovsky, M.L.2
  • 20
    • 0016740887 scopus 로고
    • Quantitative aspects of the production of superoxide radicals by phagocytizing human granulocytes
    • Weening RS, Wever R, Roos D: Quantitative aspects of the production of superoxide radicals by phagocytizing human granulocytes. J Lab Clin Med 85: 245–252, 1975
    • (1975) J Lab Clin Med , vol.85 , pp. 245-252
    • Weening, R.S.1    Wever, R.2    Roos, D.3
  • 21
    • 0016582569 scopus 로고
    • The role of superoxide anion generation in phagocytic bactericidal activity: studies with normal and chronic granulomatous disease leukocytes
    • Johnston RB Jr, Keele BB Jr, Misra HP, et al: The role of superoxide anion generation in phagocytic bactericidal activity: studies with normal and chronic granulomatous disease leukocytes. J Clin Invest 55: 1357–1372, 1975
    • (1975) J Clin Invest , vol.55 , pp. 1357-1372
    • Johnston, R.B.1    Keele, B.B.2    Misra, H.P.3
  • 22
    • 0016695109 scopus 로고
    • Complement and immunoglobulins stimulate superoxide production by human leukocytes independently of phagocytosis
    • Goldstein IM, Roos D, Kaplan HB, et al: Complement and immunoglobulins stimulate superoxide production by human leukocytes independently of phagocytosis. J Clin Invest 56: 1155–1163, 1975
    • (1975) J Clin Invest , vol.56 , pp. 1155-1163
    • Goldstein, I.M.1    Roos, D.2    Kaplan, H.B.3
  • 23
    • 0017622613 scopus 로고
    • 2: studies with normal and cytochalasin B treated cells
    • Root RK, Metcalf JA: H2O2 release from human granulocytes during phagocytosis: relationship to superoxide anion formation and cellular catabolism of H2O2: studies with normal and cytochalasin B treated cells. J Clin Invest 60: 1266–1279, 1977
    • (1977) J Clin Invest , vol.60 , pp. 1266-1279
    • Root, R.K.1    Metcalf, J.A.2
  • 24
    • 0017062603 scopus 로고
    • A comparison of the metabolic response to phagocytosis in human granulocytes and monocytes
    • Sagone AL Jr, King GW, Metz EN: A comparison of the metabolic response to phagocytosis in human granulocytes and monocytes. J Clin Invest 57: 1352–1358, 1976
    • (1976) J Clin Invest , vol.57 , pp. 1352-1358
    • Sagone, A.L.1    King, G.W.2    Metz, E.N.3
  • 25
    • 0040124585 scopus 로고
    • 2) by human eosinophils
    • Tauber AI, Goetzl EJ, Babior BM: The production of superoxide (O– 2) by human eosinophils. Blood 48: 968, 1976
    • (1976) Blood , vol.48 , pp. 968
    • Tauber, A.I.1    Goetzl, E.J.2    Babior, B.M.3
  • 26
    • 0017645571 scopus 로고
    • Functional studies on human peritoneal eosinophils
    • Klebanoff SJ, Durack DT, Rosen H, et al: Functional studies on human peritoneal eosinophils. Infect Immun 17: 167–173, 1977
    • (1977) Infect Immun , vol.17 , pp. 167-173
    • Klebanoff, S.J.1    Durack, D.T.2    Rosen, H.3
  • 28
    • 0016591134 scopus 로고
    • 2 release from human granulocytes during phagocytosis. I. Documentation, quantitation and some regulating factors
    • Root RK, Metcalf J, Oshino N, et al: H2O2 release from human granulocytes during phagocytosis. I. Documentation, quantitation and some regulating factors. J Clin Invest 55: 945–955, 1975
    • (1975) J Clin Invest , vol.55 , pp. 945-955
    • Root, R.K.1    Metcalf, J.2    Oshino, N.3
  • 29
    • 84995056760 scopus 로고
    • 2-forming system in human polymorphonuclear leukocytes (PMNs)
    • Curnutte JT, Alfred RH, Karnovsky ML, et al: Reversible stimulation of the O– 2-forming system in human polymorphonuclear leukocytes (PMNs). Clin Res 25: 337A, 1977
    • (1977) Clin Res , vol.25 , pp. 337A
    • Curnutte, J.T.1    Alfred, R.H.2    Karnovsky, M.L.3
  • 30
    • 85023692052 scopus 로고    scopus 로고
    • Superoxide production by digitonin-stimulated guinea pig granulocytes: the effects of N-ethyl maleimide, divalent cations, and glycolytic and mitochondrial inhibitors on the activation of the superoxide generating system
    • (in press)
    • Cohen HJ, Chovaniec ME: Superoxide production by digitonin-stimulated guinea pig granulocytes: the effects of N-ethyl maleimide, divalent cations, and glycolytic and mitochondrial inhibitors on the activation of the superoxide generating system. J Clin Invest (in press)
    • J Clin Invest
    • Cohen, H.J.1    Chovaniec, M.E.2
  • 31
    • 0015383043 scopus 로고
    • Role of myeloperoxidase-mediated antimicrobial systems in intact leukocytes
    • Klebanoff SJ, Hamon CB: Role of myeloperoxidase-mediated antimicrobial systems in intact leukocytes. J Reticuloendothel Soc 12: 170–196, 1972
    • (1972) J Reticuloendothel Soc , vol.12 , pp. 170-196
    • Klebanoff, S.J.1    Hamon, C.B.2
  • 32
    • 0016761189 scopus 로고
    • Production of hydrogen peroxide by phagocytizing human granulocytes
    • Homan-Müller JWT, Weening RS, Roos D: Production of hydrogen peroxide by phagocytizing human granulocytes. J Lab Clin Med 85: 198–207, 1975
    • (1975) J Lab Clin Med , vol.85 , pp. 198-207
    • Homan-Müller, J.1    Weening, R.S.2    Roos, D.3
  • 33
    • 0016240863 scopus 로고
    • Biological defense mechanisms: the effect of bacteria and serum on superoxide production by granulocytes
    • Curnutte JT, Babior BM: Biological defense mechanisms: the effect of bacteria and serum on superoxide production by granulocytes. J Clin Invest 53: 1662–1672, 1974
    • (1974) J Clin Invest , vol.53 , pp. 1662-1672
    • Curnutte, J.T.1    Babior, B.M.2
  • 34
    • 0017614782 scopus 로고
    • Evidence that the superoxide-generating system of human leukocytes is associated with the cell surface
    • Goldstein IM, Cerquiera M, Lind S, et al: Evidence that the superoxide-generating system of human leukocytes is associated with the cell surface. J Clin Invest 59: 249–254, 1977
    • (1977) J Clin Invest , vol.59 , pp. 249-254
    • Goldstein, I.M.1    Cerquiera, M.2    Lind, S.3
  • 35
    • 0017755987 scopus 로고
    • Hydrogen peroxide production in chronic granulomatous disease: a cytochemical study of reduced pyridine nucleotide oxidases
    • Briggs RT, Karnovsky ML, Karnovsky MJ: Hydrogen peroxide production in chronic granulomatous disease: a cytochemical study of reduced pyridine nucleotide oxidases. J Clin Invest 59: 1088–1098, 1977
    • (1977) J Clin Invest , vol.59 , pp. 1088-1098
    • Briggs, R.T.1    Karnovsky, M.L.2    Karnovsky, M.J.3
  • 36
    • 0001408791 scopus 로고
    • Catalases, The Enzymes
    • Second edition. Edited by PD Boyer, H Lardy, K Myrbäck. New York, Academic Press
    • Nicholls P, Schonbaum GR: Catalases, The Enzymes. Second edition. Edited by PD Boyer, H Lardy, K Myrbäck. New York, Academic Press, 1963, pp 198–200
    • (1963) , pp. 198-200
    • Nicholls, P.1    Schonbaum, G.R.2
  • 37
    • 0014669906 scopus 로고
    • Glutatione and the hexose monophosphate shunt in phagocytizing and hydrogen peroxide-treated rat leukocytes
    • Reed PW: Glutatione and the hexose monophosphate shunt in phagocytizing and hydrogen peroxide-treated rat leukocytes. J Biol Chem 244: 2459–2464, 1969
    • (1969) J Biol Chem , vol.244 , pp. 2459-2464
    • Reed, P.W.1
  • 38
    • 0016758120 scopus 로고
    • The role of superoxide anion and hydrogen peroxide in phagocytosis-associated oxidative metabolic reactions
    • Baehner RL, Murrmann SK, Davis J, et al: The role of superoxide anion and hydrogen peroxide in phagocytosis-associated oxidative metabolic reactions. J Clin Invest 56: 571–576, 1975
    • (1975) J Clin Invest , vol.56 , pp. 571-576
    • Baehner, R.L.1    Murrmann, S.K.2    Davis, J.3
  • 39
    • 0014413197 scopus 로고
    • Deficiency of reduced nicotinamide-adenine dinucleotide oxidase in chronic granulomatous disease
    • Baehner RL, Karnovsky ML: Deficiency of reduced nicotinamide-adenine dinucleotide oxidase in chronic granulomatous disease. Science 162: 1277–1279, 1968
    • (1968) Science , vol.162 , pp. 1277-1279
    • Baehner, R.L.1    Karnovsky, M.L.2
  • 40
    • 0014400858 scopus 로고
    • Quantitative nitroblue tetrazolium test in chronic granulomatous disease
    • Baehner RL, Nathan DG: Quantitative nitroblue tetrazolium test in chronic granulomatous disease. N Engl J Med 278: 971–976, 1968
    • (1968) N Engl J Med , vol.278 , pp. 971-976
    • Baehner, R.L.1    Nathan, D.G.2
  • 41
    • 0017062359 scopus 로고
    • Characterization of the enzyme defect in chronic granulomatous disease
    • Segal AW, Peters TJ: Characterization of the enzyme defect in chronic granulomatous disease. Lancet 1: 1363–1365, 1976
    • (1976) Lancet , vol.1 , pp. 1363-1365
    • Segal, A.W.1    Peters, T.J.2
  • 42
    • 0010668472 scopus 로고
    • NADPH and NADH oxidation by guinea pig polymorphonuclear leucocytes
    • Iyer GYN, Quastel JH: NADPH and NADH oxidation by guinea pig polymorphonuclear leucocytes. Can J Biochem 41: 427–434, 1963
    • (1963) Can J Biochem , vol.41 , pp. 427-434
    • Iyer, G.1    Quastel, J.H.2
  • 43
    • 0015086829 scopus 로고
    • Enzymatic basis of metabolic stimulation in leucocytes during phagocytosis: the role of activated NADPH oxidase
    • Patriarca P, Cramer R, Moncalvo S, et al: Enzymatic basis of metabolic stimulation in leucocytes during phagocytosis: the role of activated NADPH oxidase. Arch Biochem Biophys 145: 255–262, 1971
    • (1971) Arch Biochem Biophys , vol.145 , pp. 255-262
    • Patriarca, P.1    Cramer, R.2    Moncalvo, S.3
  • 44
    • 0016670732 scopus 로고
    • NADPH oxidase deficiency in X-linked chronic granulomatous disease
    • Hohn DC, Lehrer RI: NADPH oxidase deficiency in X-linked chronic granulomatous disease. J Clin Invest 55: 707–713, 1975
    • (1975) J Clin Invest , vol.55 , pp. 707-713
    • Hohn, D.C.1    Lehrer, R.I.2
  • 45
    • 0017107063 scopus 로고
    • The particulate superoxide-forming system from human neutrophils: properties of the system and further evidence supporting its participation in the respiratory burst
    • Babior BM, Curnutte JT, McMurrich BJ: The particulate superoxide-forming system from human neutrophils: properties of the system and further evidence supporting its participation in the respiratory burst. J Clin Invest 58: 989–996, 1976
    • (1976) J Clin Invest , vol.58 , pp. 989-996
    • Babior, B.M.1    Curnutte, J.T.2    McMurrich, B.J.3
  • 46
    • 0016594712 scopus 로고
    • 2 formation by leukocytes: properties of the NAD(P)H oxidase activity of intact leukocytes
    • Takanaka K, O'Brien PJ: Mechanisms of H2O2 formation by leukocytes: properties of the NAD(P)H oxidase activity of intact leukocytes. Arch Biochem Biophys 169: 436–442, 1975
    • (1975) Arch Biochem Biophys , vol.169 , pp. 436-442
    • Takanaka, K.1    O'Brien, P.J.2
  • 47
    • 0017013822 scopus 로고
    • Further characterization of NADPH oxidase activity of human polymorphonuclear leukocytes
    • McPhail LC, DeChatelet LR, Shirley PS: Further characterization of NADPH oxidase activity of human polymorphonuclear leukocytes. J Clin Invest 58: 774–780, 1976
    • (1976) J Clin Invest , vol.58 , pp. 774-780
    • McPhail, L.C.1    DeChatelet, L.R.2    Shirley, P.S.3
  • 48
    • 0017249347 scopus 로고
    • Manganese-dependent NADPH oxidation by granulocyte particles: the role of superoxide and the nonphysiological nature of the manganese requirement
    • Curnutte JT, Karnovsky ML, Babior BM: Manganese-dependent NADPH oxidation by granulocyte particles: the role of superoxide and the nonphysiological nature of the manganese requirement. J Clin Invest 57: 1059–1067, 1976
    • (1976) J Clin Invest , vol.57 , pp. 1059-1067
    • Curnutte, J.T.1    Karnovsky, M.L.2    Babior, B.M.3
  • 49
    • 0016805901 scopus 로고
    • 2
    • Patriarca P, Dri P, Kakinuma K, et al: Studies on the mechanism of metabolic stimulation in polymorphonuclear leukocytes during phagocytosis. I. Evidence for superoxide anion involvement in the oxidation of NADPH2. Biochim Biophys Acta 385: 380–386, 1975
    • (1975) Biochim Biophys Acta , vol.385 , pp. 380-386
    • Patriarca, P.1    Dri, P.2    Kakinuma, K.3
  • 50
    • 0017754240 scopus 로고
    • Superoxide-forming enzyme from human neutrophils: evidence for a flavin requirement
    • Babior BM, Kipnes RS: Superoxide-forming enzyme from human neutrophils: evidence for a flavin requirement. Blood 50: 517–524, 1977
    • (1977) Blood , vol.50 , pp. 517-524
    • Babior, B.M.1    Kipnes, R.S.2
  • 51
    • 0016814109 scopus 로고
    • Defect in pyridine nucleotide dependent superoxide production by a particulate fraction from the granulocytes of patients with chronic granulomatous disease
    • Curnutte JT, Kipnes RS, Babior BM: Defect in pyridine nucleotide dependent superoxide production by a particulate fraction from the granulocytes of patients with chronic granulomatous disease. N Engl J Med 293: 628–632, 1975
    • (1975) N Engl J Med , vol.293 , pp. 628-632
    • Curnutte, J.T.1    Kipnes, R.S.2    Babior, B.M.3
  • 52
    • 0014216865 scopus 로고
    • The role of the phagocyte in host-parasite interactions. VII. Di- and triphosphopyridine nucleotide kinetics during phagocytosis
    • Selvaraj RJ, Sbarra AJ: The role of the phagocyte in host-parasite interactions. VII. Di- and triphosphopyridine nucleotide kinetics during phagocytosis. Biochim Biophys Acta 141: 243–249, 1967
    • (1967) Biochim Biophys Acta , vol.141 , pp. 243-249
    • Selvaraj, R.J.1    Sbarra, A.J.2
  • 53
    • 0015322180 scopus 로고
    • Complete deficiency of leukocyte glucose-6-phosphate dehydrogenase with defective bactericidal activity
    • Cooper MR, DeChatelet LR, McCall CE, et al: Complete deficiency of leukocyte glucose-6-phosphate dehydrogenase with defective bactericidal activity. J Clin Invest 51: 769–778, 1972
    • (1972) J Clin Invest , vol.51 , pp. 769-778
    • Cooper, M.R.1    DeChatelet, L.R.2    McCall, C.E.3
  • 54
    • 0014124339 scopus 로고
    • Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function
    • Holmes B, Page AR, Good RA: Studies of the metabolic activity of leukocytes from patients with a genetic abnormality of phagocytic function. J Clin Invest 46: 1422–1432, 1967
    • (1967) J Clin Invest , vol.46 , pp. 1422-1432
    • Holmes, B.1    Page, A.R.2    Good, R.A.3
  • 55
    • 0017348202 scopus 로고
    • Comparison of NADH and NADPH oxidase activities in granules isolated from human polymorphonuclear leukocytes with a fluorimetric assay
    • Iverson D, DeChatelet LR, Spitznagel JK, et al: Comparison of NADH and NADPH oxidase activities in granules isolated from human polymorphonuclear leukocytes with a fluorimetric assay. J Clin Invest 59: 282–290, 1977
    • (1977) J Clin Invest , vol.59 , pp. 282-290
    • Iverson, D.1    DeChatelet, L.R.2    Spitznagel, J.K.3
  • 56
    • 0016215601 scopus 로고
    • Nitroblue-tetrazolium tests
    • Segal AW: Nitroblue-tetrazolium tests. Lancet 2: 1248–1252, 1974
    • (1974) Lancet , vol.2 , pp. 1248-1252
    • Segal, A.W.1
  • 57
    • 0014590089 scopus 로고
    • Failure of nitro blue tetrazolium reduction in the phagocytic vacuoles of leukocytes in chronic granulomatous disease
    • Nathan DG, Baehner RL, Weaver DK: Failure of nitro blue tetrazolium reduction in the phagocytic vacuoles of leukocytes in chronic granulomatous disease. J Clin Invest 48: 1895–1904, 1969
    • (1969) J Clin Invest , vol.48 , pp. 1895-1904
    • Nathan, D.G.1    Baehner, R.L.2    Weaver, D.K.3
  • 58
    • 0015699282 scopus 로고
    • Re-evaluation of nitroblue tetrazolium tests
    • Segal AW, Trustey SF, Levi AJ: Re-evaluation of nitroblue tetrazolium tests. Lancet 2: 879–883, 1973
    • (1973) Lancet , vol.2 , pp. 879-883
    • Segal, A.W.1    Trustey, S.F.2    Levi, A.J.3
  • 59
    • 0017159513 scopus 로고
    • The biochemical basis of nitroblue tetrazolium reduction in normal human and chronic granulomatous disease polymorphonuclear leukocytes
    • Baehner RL, Boxer LA, Davis J: The biochemical basis of nitroblue tetrazolium reduction in normal human and chronic granulomatous disease polymorphonuclear leukocytes. Blood 48: 309–313, 1976
    • (1976) Blood , vol.48 , pp. 309-313
    • Baehner, R.L.1    Boxer, L.A.2    Davis, J.3
  • 60
    • 0015524885 scopus 로고
    • Evidence for the generation of an electronic excitation state(s) in human polymorphonuclear leukocytes and its participation in bactericidal activity
    • Allen RC, Stjernholm RL, Steele RH: Evidence for the generation of an electronic excitation state(s) in human polymorphonuclear leukocytes and its participation in bactericidal activity. Biochem Biophys Res Commun 47: 679–684, 1972
    • (1972) Biochem Biophys Res Commun , vol.47 , pp. 679-684
    • Allen, R.C.1    Stjernholm, R.L.2    Steele, R.H.3
  • 61
    • 0016253876 scopus 로고
    • Inhibition of phagocytosis-associated chemiluminescence by superoxide dismutase
    • Webb LS, Keele BB Jr, Johnston RB Jr: Inhibition of phagocytosis-associated chemiluminescence by superoxide dismutase. Infect Immun 9: 1051–1056, 1974
    • (1974) Infect Immun , vol.9 , pp. 1051-1056
    • Webb, L.S.1    Keele, B.B.2    Johnston, R.B.3
  • 62
    • 0017119679 scopus 로고
    • The origin of the chemiluminescence of phagocytosing granulocytes
    • Cheson BD, Christensen RL, Sperling R, et al: The origin of the chemiluminescence of phagocytosing granulocytes. J Clin Invest 58: 789–796, 1976
    • (1976) J Clin Invest , vol.58 , pp. 789-796
    • Cheson, B.D.1    Christensen, R.L.2    Sperling, R.3
  • 63
    • 0015578408 scopus 로고
    • Impaired chemiluminescence during phagocytosis of opsonized bacteria
    • Stjernholm RL, Allen RC, Steele RH, et al: Impaired chemiluminescence during phagocytosis of opsonized bacteria. Infect Immun 7: 313–314, 1973
    • (1973) Infect Immun , vol.7 , pp. 313-314
    • Stjernholm, R.L.1    Allen, R.C.2    Steele, R.H.3
  • 64
    • 0016590865 scopus 로고
    • Biological defense mechanisms: evidence for the participation of superoxide in bacterial killing by xanthine oxidase
    • Babior BM, Curnutte JT, Kipnes RS: Biological defense mechanisms: evidence for the participation of superoxide in bacterial killing by xanthine oxidase. J Lab Clin Med 85: 235–244, 1975
    • (1975) J Lab Clin Med , vol.85 , pp. 235-244
    • Babior, B.M.1    Curnutte, J.T.2    Kipnes, R.S.3
  • 65
    • 0016660853 scopus 로고
    • Catalase, superoxide dismutase, and virulence of Staphylococcus aureus: in vitro and in vivo studies with emphasis on staphylococcal-leukocyte interaction
    • Mandell GL: Catalase, superoxide dismutase, and virulence of Staphylococcus aureus: in vitro and in vivo studies with emphasis on staphylococcal-leukocyte interaction. J Clin Invest 55: 561–566, 1975
    • (1975) J Clin Invest , vol.55 , pp. 561-566
    • Mandell, G.L.1
  • 66
    • 0015946751 scopus 로고
    • Oxygen metabolism in Lactobacillus plantarum
    • Gregory EM, Fridovich I: Oxygen metabolism in Lactobacillus plantarum. J Bacteriol 117: 166–169, 1974
    • (1974) J Bacteriol , vol.117 , pp. 166-169
    • Gregory, E.M.1    Fridovich, I.2
  • 67
    • 0015832348 scopus 로고
    • Superoxide dismutases of Escherichia coli: intracellular localization and functions
    • Gregory EM, Yost FJ Jr, Fridovich I: Superoxide dismutases of Escherichia coli: intracellular localization and functions. J Bacteriol 115: 987–991, 1973
    • (1973) J Bacteriol , vol.115 , pp. 987-991
    • Gregory, E.M.1    Yost, F.J.2    Fridovich, I.3
  • 68
    • 0016175884 scopus 로고
    • Bactericidal activity of metal-mediated peroxide-ascorbate systems
    • Drath DB, Karnovsky ML: Bactericidal activity of metal-mediated peroxide-ascorbate systems. Infect Immun 10: 1077–1083, 1974
    • (1974) Infect Immun , vol.10 , pp. 1077-1083
    • Drath, D.B.1    Karnovsky, M.L.2
  • 69
    • 0242271567 scopus 로고
    • The molecular weight of myeloperoxidase
    • Ehrenberg A, Agner K: The molecular weight of myeloperoxidase. Acta Chem Scand 12: 95, 1958
    • (1958) Acta Chem Scand , vol.12 , pp. 95
    • Ehrenberg, A.1    Agner, K.2
  • 70
    • 0014352707 scopus 로고
    • Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of bone marrow cells
    • Bainton DF, Farquhar MG: Differences in enzyme content of azurophil and specific granules of polymorphonuclear leukocytes. II. Cytochemistry and electron microscopy of bone marrow cells. J Cell Biol 39: 299–317, 1968
    • (1968) J Cell Biol , vol.39 , pp. 299-317
    • Bainton, D.F.1    Farquhar, M.G.2
  • 71
    • 0014559249 scopus 로고
    • Leukocyte myeloperoxidase deficiency and disseminated candidiasis: the role of myeloperoxidase in resistance to Candida infection
    • Lehrer RI, Cline MJ: Leukocyte myeloperoxidase deficiency and disseminated candidiasis: the role of myeloperoxidase in resistance to Candida infection. J Clin Invest 48: 1478–1488, 1969
    • (1969) J Clin Invest , vol.48 , pp. 1478-1488
    • Lehrer, R.I.1    Cline, M.J.2
  • 72
    • 0014966717 scopus 로고
    • Myeloperoxidase deficiency: immunological study of a genetic leukocyte defect
    • Salmon SE, Cline MJ, Schultz J, et al: Myeloperoxidase deficiency: immunological study of a genetic leukocyte defect. N Engl J Med 282: 250–253, 1970
    • (1970) N Engl J Med , vol.282 , pp. 250-253
    • Salmon, S.E.1    Cline, M.J.2    Schultz, J.3
  • 73
    • 0014167106 scopus 로고
    • Iodination of bacteria: a bactericidal mechanism
    • Klebanoff SJ: Iodination of bacteria: a bactericidal mechanism. J Exp Med 126: 1063–1078, 1967
    • (1967) J Exp Med , vol.126 , pp. 1063-1078
    • Klebanoff, S.J.1
  • 74
    • 0014292067 scopus 로고
    • Myeloperoxidase-halide-hydrogen peroxide antibacterial system
    • Klebanoff: Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J Bacteriol 95: 2131–2138, 1968
    • (1968) J Bacteriol , vol.95 , pp. 2131-2138
  • 75
    • 0017240322 scopus 로고
    • Studies on the chlorinating activity of myeloperoxidase
    • Harrison JE, Schultz J: Studies on the chlorinating activity of myeloperoxidase. J Biol Chem 251: 1371–1374, 1976
    • (1976) J Biol Chem , vol.251 , pp. 1371-1374
    • Harrison, J.E.1    Schultz, J.2
  • 76
    • 0001645466 scopus 로고
    • A peroxidase-mediated antimicrobial system in leukocytes
    • Klebanoff SJ: A peroxidase-mediated antimicrobial system in leukocytes. J Clin Invest 46: 1078, 1967
    • (1967) J Clin Invest , vol.46 , pp. 1078
    • Klebanoff, S.J.1
  • 77
    • 0014147985 scopus 로고
    • Role of the phagocyte in host-parasite interactions. XII. Hydrogen peroxide-myeloperoxidase bactericidal system in the phagocyte
    • McRipley RJ, Sbarra AJ: Role of the phagocyte in host-parasite interactions. XII. Hydrogen peroxide-myeloperoxidase bactericidal system in the phagocyte. J Bacteriol 94: 1425–1430, 1967
    • (1967) J Bacteriol , vol.94 , pp. 1425-1430
    • McRipley, R.J.1    Sbarra, A.J.2
  • 78
    • 0015847346 scopus 로고
    • Iodinating ability of various leukocytes and their bactericidal activity
    • Simmons SR, Karnovsky ML: Iodinating ability of various leukocytes and their bactericidal activity. J Exp Med 138: 44–63, 1973
    • (1973) J Exp Med , vol.138 , pp. 44-63
    • Simmons, S.R.1    Karnovsky, M.L.2
  • 79
    • 0015214826 scopus 로고
    • Quantitative leukocyte iodination
    • Pincus SH, Klebanoff SJ: Quantitative leukocyte iodination. N Engl J Med 284: 744–750, 1971
    • (1971) N Engl J Med , vol.284 , pp. 744-750
    • Pincus, S.H.1    Klebanoff, S.J.2
  • 80
    • 0016798148 scopus 로고
    • Chlorinating ability of human phagocytosing leukocytes
    • Zgliczynski JM, Stelmaszynska T: Chlorinating ability of human phagocytosing leukocytes. Eur J Biochem 56: 157–162, 1975
    • (1975) Eur J Biochem , vol.56 , pp. 157-162
    • Zgliczynski, J.M.1    Stelmaszynska, T.2
  • 81
    • 0015100558 scopus 로고
    • The effects of ascorbic acid on bactericidal mechanisms of neutrophils
    • McCall CE, DeChatelet LR, Cooper MR, et al: The effects of ascorbic acid on bactericidal mechanisms of neutrophils. J Infect Dis 124: 194–198, 1971
    • (1971) J Infect Dis , vol.124 , pp. 194-198
    • McCall, C.E.1    DeChatelet, L.R.2    Cooper, M.R.3
  • 82
    • 0014280629 scopus 로고
    • Myeloperoxidase of human leukaemic leukocytes: oxidation of amino acids in the presence of hydrogen peroxide
    • Zgliczynski JM, Stelmaszynska T, Ostrowski W, et al: Myeloperoxidase of human leukaemic leukocytes: oxidation of amino acids in the presence of hydrogen peroxide. Eur J Biochem 4: 540–547, 1968
    • (1968) Eur J Biochem , vol.4 , pp. 540-547
    • Zgliczynski, J.M.1    Stelmaszynska, T.2    Ostrowski, W.3
  • 83
    • 0014802559 scopus 로고
    • 2-dependent decarboxylation and deamination by myeloperoxidase and its relationship to antimicrobial activity
    • Strauss RR, Paul BB, Jacobs AA, et al: Role of the phagocyte in host-parasite interactions. XXII. H2O2-dependent decarboxylation and deamination by myeloperoxidase and its relationship to antimicrobial activity. J Reticuloendothel Soc 7: 754–761, 1970
    • (1970) J Reticuloendothel Soc , vol.7 , pp. 754-761
    • Strauss, R.R.1    Paul, B.B.2    Jacobs, A.A.3
  • 84
    • 0001394061 scopus 로고
    • 2-Cl−-mediated aldehyde formation and its relationship to antimicrobial activity
    • Strauss: Role of the phagocyte in host-parasite interactions. XXVII. Myeloperoxidase-H2O2-Cl−-mediated aldehyde formation and its relationship to antimicrobial activity. Infect Immun 3: 595–602, 1971
    • (1971) Infect Immun , vol.3 , pp. 595-602
  • 85
    • 18244372607 scopus 로고
    • 2-chloride antimicrobial system: a possible in vivo mechanism of action
    • Paul BB, Jacobs AA, Strauss RR, et al: Role of the phagocyte in host-parasite interactions. XXIV. Aldehyde generation by the myeloperoxidase dase-H2O2-chloride antimicrobial system: a possible in vivo mechanism of action. Infect Immun 2: 414–418, 1970
    • (1970) Infect Immun , vol.2 , pp. 414-418
    • Paul, B.B.1    Jacobs, A.A.2    Strauss, R.R.3
  • 86
    • 0003804520 scopus 로고
    • Reactivity of the Hydroxyl Radical in Aqueous Solutions
    • Washington, DC, Government Printing Office
    • Dorfman LM, Adams GE: Reactivity of the Hydroxyl Radical in Aqueous Solutions. Washington, DC, Government Printing Office, 1973, pp 4–6
    • (1973) , pp. 4-6
    • Dorfman, L.M.1    Adams, G.E.2
  • 87
    • 0014962758 scopus 로고
    • A mechanism for the production of ethylene from methional: the generation of hydroxyl radical by xanthine oxidase
    • Beauchamp C, Fridovich I: A mechanism for the production of ethylene from methional: the generation of hydroxyl radical by xanthine oxidase. J Biol Chem 245: 4641–4646, 1970
    • (1970) J Biol Chem , vol.245 , pp. 4641-4646
    • Beauchamp, C.1    Fridovich, I.2
  • 88
    • 0017648208 scopus 로고
    • Evidence for hydroxyl radical generation by human monocytes
    • Weiss SJ, King GW, LoBuglio AF: Evidence for hydroxyl radical generation by human monocytes. J Clin Invest 60: 370–373, 1977
    • (1977) J Clin Invest , vol.60 , pp. 370-373
    • Weiss, S.J.1    King, G.W.2    LoBuglio, A.F.3
  • 89
    • 0017736305 scopus 로고
    • Evidence for hydroxyl radical production by human neutrophils
    • Tauber AI, Babior BM: Evidence for hydroxyl radical production by human neutrophils. J Clin Invest 60: 374–379, 1977
    • (1977) J Clin Invest , vol.60 , pp. 374-379
    • Tauber, A.I.1    Babior, B.M.2
  • 91
    • 0016302852 scopus 로고
    • Lipid peroxidation by human blood phagocytes
    • Stossel TP, Mason RJ, Smith AL: Lipid peroxidation by human blood phagocytes. J Clin Invest 54: 638–645, 1974
    • (1974) J Clin Invest , vol.54 , pp. 638-645
    • Stossel, T.P.1    Mason, R.J.2    Smith, A.L.3
  • 92
    • 0016328006 scopus 로고
    • Lipid peroxidation in the killing of phagocytized pneumococci
    • Shohet SB, Pitt J, Baehner RL, et al: Lipid peroxidation in the killing of phagocytized pneumococci. Infect Immun 10: 1321–1328, 1974
    • (1974) Infect Immun , vol.10 , pp. 1321-1328
    • Shohet, S.B.1    Pitt, J.2    Baehner, R.L.3
  • 93
    • 33947291445 scopus 로고
    • Physical and chemical properties of singlet molecular oxygen
    • Kearns DR: Physical and chemical properties of singlet molecular oxygen. Chem Rev 71: 395–427, 1971
    • (1971) Chem Rev , vol.71 , pp. 395-427
    • Kearns, D.R.1
  • 94
    • 0005610584 scopus 로고
    • A photoelectric method for the measurement of spectra of light sources of rapidly varying intensities
    • Seliger HH: A photoelectric method for the measurement of spectra of light sources of rapidly varying intensities. Anal Biochem 1: 60–65, 1960
    • (1960) Anal Biochem , vol.1 , pp. 60-65
    • Seliger, H.H.1
  • 95
    • 0016719209 scopus 로고
    • Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system
    • Kellogg EW III, Fridovich I: Superoxide, hydrogen peroxide, and singlet oxygen in lipid peroxidation by a xanthine oxidase system. J Biol Chem 250: 8812–8817, 1975
    • (1975) J Biol Chem , vol.250 , pp. 8812-8817
    • Kellogg, E.W.1    Fridovich, I.2
  • 96
    • 0000891876 scopus 로고
    • Singlet molecular oxygen from superoxide anion and sensitized fluorescence of organic molecules
    • Khan AU: Singlet molecular oxygen from superoxide anion and sensitized fluorescence of organic molecules. Science 168: 476–477, 1970
    • (1970) Science , vol.168 , pp. 476-477
    • Khan, A.U.1
  • 97
    • 85023683639 scopus 로고    scopus 로고
    • Biological roles of singlet oxygen, Singlet Oxygen
    • Edited by HH Wasserman, RW Murray. New York, Academic Press (in press)
    • Krinsky NI: Biological roles of singlet oxygen, Singlet Oxygen. Edited by HH Wasserman, RW Murray. New York, Academic Press (in press)
    • Krinsky, N.I.1
  • 98
    • 0003909732 scopus 로고
    • Isotope Effects on Reaction Rates
    • New York, Ronald Press
    • Melander LC: Isotope Effects on Reaction Rates. New York, Ronald Press, 1960
    • (1960)
    • Melander, L.C.1
  • 99
    • 0016167733 scopus 로고
    • Singlet excited oxygen as a mediator of the antibacterial action of leukocytes
    • Krinsky NI: Singlet excited oxygen as a mediator of the antibacterial action of leukocytes. Science 186: 363–365, 1974
    • (1974) Science , vol.186 , pp. 363-365
    • Krinsky, N.I.1
  • 100
    • 0017642364 scopus 로고
    • Formation of singlet oxygen by the myeloperoxidase-mediated antimicrobial system
    • Rosen H, Klebanoff SJ: Formation of singlet oxygen by the myeloperoxidase-mediated antimicrobial system. J Biol Chem 252: 4803–4810, 1977
    • (1977) J Biol Chem , vol.252 , pp. 4803-4810
    • Rosen, H.1    Klebanoff, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.