메뉴 건너뛰기




Volumn 105, Issue 3-4, 2003, Pages 232-240

The protistan parasite Perkinsus marinus is resistant to selected reactive oxygen species

Author keywords

Alveolata; Hydrogen peroxide; Hypochlorite; Oxidative stress; Perkinsus marinus; Peroxidase; Superoxide; Vibrio splendidus

Indexed keywords

CATALASE; HYDROGEN PEROXIDE; HYPOCHLORITE; PEROXIDASE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE;

EID: 1342265409     PISSN: 00144894     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exppara.2003.12.012     Document Type: Article
Times cited : (51)

References (59)
  • 1
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H. Catalase in vitro. Methods Enzymol. 105:1984;121-126.
    • (1984) Methods Enzymol. , vol.105 , pp. 121-126
    • Aebi, H.1
  • 2
    • 0038362437 scopus 로고    scopus 로고
    • Superoxide dismutases from the oyster parasite Perkinsus marinus: Purification, biochemical characterization, and development of a plate microassay for activity
    • Ahmed H., Schott E.J., Silva A.M., Vasta G.R. Superoxide dismutases from the oyster parasite Perkinsus marinus: purification, biochemical characterization, and development of a plate microassay for activity. Anal. Biochem. 318:2003;132-141.
    • (2003) Anal. Biochem. , vol.318 , pp. 132-141
    • Ahmed, H.1    Schott, E.J.2    Silva, A.M.3    Vasta, G.R.4
  • 3
    • 0028316410 scopus 로고
    • Variation in hydrogen peroxide sensitivity between different strains of Neisseria gonorrhoeae is dependent on factors in addition to catalase activity
    • Alcorn T.M., Zheng H.Y., Gunther M.R., Hassett D.J., Cohen M.S. Variation in hydrogen peroxide sensitivity between different strains of Neisseria gonorrhoeae is dependent on factors in addition to catalase activity. Infect. Immun. 62:1994;2136-2140.
    • (1994) Infect. Immun. , vol.62 , pp. 2136-2140
    • Alcorn, T.M.1    Zheng, H.Y.2    Gunther, M.R.3    Hassett, D.J.4    Cohen, M.S.5
  • 4
    • 0028055996 scopus 로고
    • Separate assays specific for ascorbate peroxidase and guaiacol peroxidase and for the chloroplastic and cytosolic isozymes of ascorbate peroxidase in plants
    • Amako K., Chen G.-X., Asada K. Separate assays specific for ascorbate peroxidase and guaiacol peroxidase and for the chloroplastic and cytosolic isozymes of ascorbate peroxidase in plants. Plant Cell Physiol. 35:1994;497-504.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 497-504
    • Amako, K.1    Chen, G.-X.2    Asada, K.3
  • 5
    • 0032608676 scopus 로고    scopus 로고
    • Perkinsus marinus secretory products modulate superoxide anion production by oyster (Crassostrea virginica) haemocytes
    • Anderson R.S. Perkinsus marinus secretory products modulate superoxide anion production by oyster (Crassostrea virginica) haemocytes. Fish Shellfish Immunol. 9:1999;51-60.
    • (1999) Fish Shellfish Immunol. , vol.9 , pp. 51-60
    • Anderson, R.S.1
  • 6
    • 0030766319 scopus 로고    scopus 로고
    • Effect of in vitro exposure to tributyltin on generation of oxygen metabolites by oyster hemocytes
    • Anderson R.S., Brubacher L.L., Calvo L.M., Burreson E.M., Unger M.A. Effect of in vitro exposure to tributyltin on generation of oxygen metabolites by oyster hemocytes. Environ. Res. 74:1997;84-90.
    • (1997) Environ. Res. , vol.74 , pp. 84-90
    • Anderson, R.S.1    Brubacher, L.L.2    Calvo, L.M.3    Burreson, E.M.4    Unger, M.A.5
  • 7
    • 0001765016 scopus 로고
    • Increased reactive oxygen intermediate production by hemocytes withdrawn from Crassostrea virginica infected with Perkinsus marinus
    • Anderson R.S., Paynter K.T., Burreson E.M. Increased reactive oxygen intermediate production by hemocytes withdrawn from Crassostrea virginica infected with Perkinsus marinus. Biol. Bull. Mar. Biol. Lab. Woods Hole. 183:1992;476-481.
    • (1992) Biol. Bull. Mar. Biol. Lab. Woods Hole , vol.183 , pp. 476-481
    • Anderson, R.S.1    Paynter, K.T.2    Burreson, E.M.3
  • 8
    • 0024711717 scopus 로고
    • Fine structure of Perkinsus atlanticus n. sp. (Apicomplexa, Perkinsea) parasite of the clam Ruditapes decussatus from Portugal
    • Azevedo C. Fine structure of Perkinsus atlanticus n. sp. (Apicomplexa, Perkinsea) parasite of the clam Ruditapes decussatus from Portugal. J. Parasitol. 75:1989;627-635.
    • (1989) J. Parasitol. , vol.75 , pp. 627-635
    • Azevedo, C.1
  • 9
    • 0030856488 scopus 로고    scopus 로고
    • Levels of DNA strand breaks and superoxide in phorbol ester-treated human granulocytes
    • Birnboim H.C., Sandhu J. Levels of DNA strand breaks and superoxide in phorbol ester-treated human granulocytes. J. Cell. Biochem. 66:1997;219-228.
    • (1997) J. Cell. Biochem. , vol.66 , pp. 219-228
    • Birnboim, H.C.1    Sandhu, J.2
  • 10
    • 0023503598 scopus 로고
    • Relationship of bacterial growth phase to killing of Listeria monocytogenes by oxidative agents generated by neutrophils and enzyme systems
    • Bortolussi R., Vandenbroucke-Grauls C.M., van Asbeck B.S., Verhoef J. Relationship of bacterial growth phase to killing of Listeria monocytogenes by oxidative agents generated by neutrophils and enzyme systems. Infect. Immun. 55:1987;3197-3203.
    • (1987) Infect. Immun. , vol.55 , pp. 3197-3203
    • Bortolussi, R.1    Vandenbroucke-Grauls, C.M.2    Van Asbeck, B.S.3    Verhoef, J.4
  • 12
    • 0031946169 scopus 로고    scopus 로고
    • A comparison of the chemiluminescent response of Crassostrea virginica and Morone saxatilis phagocytes to zymosan and viable Listonella anguillarum
    • Bramble L.H., Anderson R.S. A comparison of the chemiluminescent response of Crassostrea virginica and Morone saxatilis phagocytes to zymosan and viable Listonella anguillarum. Dev. Comp. Immunol. 22:1998;55-61.
    • (1998) Dev. Comp. Immunol. , vol.22 , pp. 55-61
    • Bramble, L.H.1    Anderson, R.S.2
  • 13
    • 0019532613 scopus 로고
    • DNA strand scission by enzymically generated oxygen radicals
    • Brawn K., Fridovich I. DNA strand scission by enzymically generated oxygen radicals. Arch. Biochem. Biophys. 206:1981;414-419.
    • (1981) Arch. Biochem. Biophys. , vol.206 , pp. 414-419
    • Brawn, K.1    Fridovich, I.2
  • 14
    • 0036187251 scopus 로고    scopus 로고
    • Cryptophagus subtilis: A new parasite of cryptophytes affiliated with the Perkinsozoa lineage
    • Brugerolle G. Cryptophagus subtilis: a new parasite of cryptophytes affiliated with the Perkinsozoa lineage. Eur. J. Protistol. 37:2002;379-390.
    • (2002) Eur. J. Protistol. , vol.37 , pp. 379-390
    • Brugerolle, G.1
  • 15
    • 1342294179 scopus 로고    scopus 로고
    • Antioxidant enzymes, potential virulent factors, in different strains of the oyster protozoan parasite, Perkinsus marinus
    • Chu F.L., Volety A.K., Armknecht S. Antioxidant enzymes, potential virulent factors, in different strains of the oyster protozoan parasite, Perkinsus marinus. J. Shellfish Res. 17:1998.
    • (1998) J. Shellfish Res. , vol.17
    • Chu, F.L.1    Volety, A.K.2    Armknecht, S.3
  • 16
    • 0029014185 scopus 로고
    • Inactivation of an animal and a fungal catalase by hydrogen peroxide
    • DeLuca D.C., Dennis R., Smith W.G. Inactivation of an animal and a fungal catalase by hydrogen peroxide. Arch. Biochem. Biophys. 1995;129-134.
    • (1995) Arch. Biochem. Biophys. , pp. 129-134
    • Deluca, D.C.1    Dennis, R.2    Smith, W.G.3
  • 17
    • 0033566114 scopus 로고    scopus 로고
    • Reactive oxygen species are partially involved in the bacteriocidal action of hypochlorous acid
    • Dukan S., Belkin S., Touati D. Reactive oxygen species are partially involved in the bacteriocidal action of hypochlorous acid. Arch. Biochem. Biophys. 367:1999;311-316.
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 311-316
    • Dukan, S.1    Belkin, S.2    Touati, D.3
  • 18
    • 0023224149 scopus 로고
    • Role of myeloperoxidase in the killing of Naegleria fowleri by lymphokine-altered human neutrophils
    • Ferrante A., Hill N.L., Abell T.J., Pruul H. Role of myeloperoxidase in the killing of Naegleria fowleri by lymphokine-altered human neutrophils. Infect. Immun. 55:1987;1047-1050.
    • (1987) Infect. Immun. , vol.55 , pp. 1047-1050
    • Ferrante, A.1    Hill, N.L.2    Abell, T.J.3    Pruul, H.4
  • 19
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner P.R., Fridovich I. Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266:1991;19328-19333.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 20
    • 23444454190 scopus 로고
    • Continuous in vitro culture of the eastern oyster parasite Perkinsus marinus
    • Gauthier J.D., Vasta G.R. Continuous in vitro culture of the eastern oyster parasite Perkinsus marinus. J. Invertebr. Pathol. 62:1993;321-323.
    • (1993) J. Invertebr. Pathol. , vol.62 , pp. 321-323
    • Gauthier, J.D.1    Vasta, G.R.2
  • 22
    • 0027200066 scopus 로고
    • Phylogenetic position of the genus Perkinsus (Protista, Apicomplexa) based on small subunit ribosomal RNA
    • Goggin C.L., Barker S.C. Phylogenetic position of the genus Perkinsus (Protista, Apicomplexa) based on small subunit ribosomal RNA. Mol. Biochem. Parasitol. 60:1993;65-70.
    • (1993) Mol. Biochem. Parasitol. , vol.60 , pp. 65-70
    • Goggin, C.L.1    Barker, S.C.2
  • 23
    • 0002456977 scopus 로고
    • Measurement of oxidative activity in hemocytes of the Pacific razor clam, Siliqua patula, and the oyster, Crassostrea gigas, using lucigenin- and luminol-dependent chemiluminescence
    • Greger E.A., Drum A.S., Elston R.A. Measurement of oxidative activity in hemocytes of the Pacific razor clam, Siliqua patula, and the oyster, Crassostrea gigas, using lucigenin- and luminol-dependent chemiluminescence. J. Invertebr. Pathol. 65:1995;48-60.
    • (1995) J. Invertebr. Pathol. , vol.65 , pp. 48-60
    • Greger, E.A.1    Drum, A.S.2    Elston, R.A.3
  • 24
    • 0035052928 scopus 로고    scopus 로고
    • Killing of Schistosoma mansoni sporocysts by hemocytes from resistant Biomphalaria glabrata: Role of reactive oxygen species
    • Hahn U.K., Bender R.C., Bayne C.J. Killing of Schistosoma mansoni sporocysts by hemocytes from resistant Biomphalaria glabrata: role of reactive oxygen species. J. Parasitol. 87:2001;292-299.
    • (2001) J. Parasitol. , vol.87 , pp. 292-299
    • Hahn, U.K.1    Bender, R.C.2    Bayne, C.J.3
  • 26
    • 0024321691 scopus 로고
    • Susceptibility of Eimeria bovis and Toxoplasma gondii to oxygen intermediates and a new mathematical model for parasite killing
    • Hughes H.P., Boik R.J., Gerhardt S.A., Speer C.A. Susceptibility of Eimeria bovis and Toxoplasma gondii to oxygen intermediates and a new mathematical model for parasite killing. J. Parasitol. 75:1989;489-497.
    • (1989) J. Parasitol. , vol.75 , pp. 489-497
    • Hughes, H.P.1    Boik, R.J.2    Gerhardt, S.A.3    Speer, C.A.4
  • 27
    • 0023009128 scopus 로고
    • The effect of oxygen-dependent antimicrobial systems on strains of Legionella pneumophila of different virulence
    • Jepras R.I., Fitzgeorge R.B. The effect of oxygen-dependent antimicrobial systems on strains of Legionella pneumophila of different virulence. J. Hyg. (Lond.). 97:1986;61-69.
    • (1986) J. Hyg. (Lond.) , vol.97 , pp. 61-69
    • Jepras, R.I.1    Fitzgeorge, R.B.2
  • 28
    • 0029881550 scopus 로고    scopus 로고
    • Survival of Vibrio parahaemolyticus at low temperatures under starvation conditions and subsequent resuscitation of viable, nonculturable cells
    • Jiang X., Chai T.J. Survival of Vibrio parahaemolyticus at low temperatures under starvation conditions and subsequent resuscitation of viable, nonculturable cells. Appl. Environ. Microbiol. 62:1996;1300-1305.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1300-1305
    • Jiang, X.1    Chai, T.J.2
  • 29
    • 0026632930 scopus 로고
    • Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein
    • Jiang Z.Y., Hunt J.V., Wolff S.P. Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein. Anal. Biochem. 202:1992;384-389.
    • (1992) Anal. Biochem. , vol.202 , pp. 384-389
    • Jiang, Z.Y.1    Hunt, J.V.2    Wolff, S.P.3
  • 30
    • 0036194027 scopus 로고    scopus 로고
    • A potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of Gram-negative bacteria
    • Korshunov S.S., Imlay J.A. A potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of Gram-negative bacteria. Mol. Microbiol. 43:2002;95-106.
    • (2002) Mol. Microbiol. , vol.43 , pp. 95-106
    • Korshunov, S.S.1    Imlay, J.A.2
  • 31
    • 0028889725 scopus 로고
    • In vitro interaction of Perkinsus marinus merozoites with eastern and Pacific oyster hemocytes
    • La Peyre J.F., Chu F.L., Vogelbein W.K. In vitro interaction of Perkinsus marinus merozoites with eastern and Pacific oyster hemocytes. Dev. Comp. Immunol. 19:1995;291-304.
    • (1995) Dev. Comp. Immunol. , vol.19 , pp. 291-304
    • La Peyre, J.F.1    Chu, F.L.2    Vogelbein, W.K.3
  • 32
    • 0035850432 scopus 로고    scopus 로고
    • A Vibrio splendidus strain is associated with summer mortality of juvenile oysters Crassostrea gigas in the Bay of Morlaix (North Brittany, France)
    • Lacoste A., Jalabert F., Malham S., Cueff A., Gelebart F., Cordevant C., Lange M., Poulet S.A. A Vibrio splendidus strain is associated with summer mortality of juvenile oysters Crassostrea gigas in the Bay of Morlaix (North Brittany, France). Dis. Aquat. Organ. 46:2001;139-145.
    • (2001) Dis. Aquat. Organ , vol.46 , pp. 139-145
    • Lacoste, A.1    Jalabert, F.2    Malham, S.3    Cueff, A.4    Gelebart, F.5    Cordevant, C.6    Lange, M.7    Poulet, S.A.8
  • 33
    • 0000955255 scopus 로고
    • A new Perkinsus species (Apicomplexa, Perkinsea) from the abalone Haliotis ruber
    • Lester R.J.G., Davis G.H.G. A new Perkinsus species (Apicomplexa, Perkinsea) from the abalone Haliotis ruber. J. Invertebr. Pathol. 37:1981;181-187.
    • (1981) J. Invertebr. Pathol. , vol.37 , pp. 181-187
    • Lester, R.J.G.1    Davis, G.H.G.2
  • 34
    • 0001416342 scopus 로고
    • Perkinsus gen.n., other new taxa in the protozoan phylum Apicomplexa
    • Levine N.D. Perkinsus gen.n., other new taxa in the protozoan phylum Apicomplexa. J. Parasitol. 64:1978;549.
    • (1978) J. Parasitol. , vol.64 , pp. 549
    • Levine, N.D.1
  • 35
    • 0030458544 scopus 로고    scopus 로고
    • Antioxidant defense mechanisms in parasitic protozoa
    • Mehlotra R.K. Antioxidant defense mechanisms in parasitic protozoa. Crit. Rev. Microbiol. 22:1996;295-314.
    • (1996) Crit. Rev. Microbiol. , vol.22 , pp. 295-314
    • Mehlotra, R.K.1
  • 36
    • 0000442305 scopus 로고
    • Susceptibility of diploid and triploid pacific oysters Crassostrea gigas (Thunberg, 1793) and eastern oysters, Crassostrea virginica (Gmelin, 1791), to Perkinsus marinus
    • Meyers J.A., Burreson E.M., Barber B.J., Mann R. Susceptibility of diploid and triploid pacific oysters Crassostrea gigas (Thunberg, 1793) and eastern oysters, Crassostrea virginica (Gmelin, 1791), to Perkinsus marinus. J. Shellfish Res. 10:1991;433-437.
    • (1991) J. Shellfish Res. , vol.10 , pp. 433-437
    • Meyers, J.A.1    Burreson, E.M.2    Barber, B.J.3    Mann, R.4
  • 37
    • 0036092342 scopus 로고    scopus 로고
    • Characterization and immunolocalization of a main proteinaceous component of the cell wall of the protozoan parasite Perkinsus atlanticus
    • Montes J.F., Durfort M., Llado A., Garcia-Valero J. Characterization and immunolocalization of a main proteinaceous component of the cell wall of the protozoan parasite Perkinsus atlanticus. Parasitology. 124:2002;477-484.
    • (2002) Parasitology , vol.124 , pp. 477-484
    • Montes, J.F.1    Durfort, M.2    Llado, A.3    Garcia-Valero, J.4
  • 38
    • 0018675769 scopus 로고
    • Macrophage oxygen-dependent antimicrobial activity. I. Susceptibility of Toxoplasma gondii to oxygen intermediates
    • Murray H., Cohn Z. Macrophage oxygen-dependent antimicrobial activity. I. Susceptibility of Toxoplasma gondii to oxygen intermediates. J. Exp. Med. 150:1979;938-949.
    • (1979) J. Exp. Med. , vol.150 , pp. 938-949
    • Murray, H.1    Cohn, Z.2
  • 39
    • 0021845549 scopus 로고
    • In vitro production of hydrogen peroxide by the amoebocytes of the scallop, Patinopecten yessoensis (Jay)
    • Nakamura M., Mori K., Inooka S., Nomura T. In vitro production of hydrogen peroxide by the amoebocytes of the scallop, Patinopecten yessoensis (Jay). Dev. Comp. Immunol. 9:1985;407-417.
    • (1985) Dev. Comp. Immunol. , vol.9 , pp. 407-417
    • Nakamura, M.1    Mori, K.2    Inooka, S.3    Nomura, T.4
  • 40
    • 0033569523 scopus 로고    scopus 로고
    • Parvilucifera infectans Norén et Moestrup gen. et sp. nov. (Perkinsozoa phylum nov.): A parasitic flagellate capable of killing toxic microalgae
    • Norén F., Moestrup Ø., Rehnstam-Holm A.-S. Parvilucifera infectans Norén et Moestrup gen. et sp. nov. (Perkinsozoa phylum nov.): a parasitic flagellate capable of killing toxic microalgae. Vet. Parasitol. 35:1999;233-254.
    • (1999) Vet. Parasitol. , vol.35 , pp. 233-254
    • Norén, F.1    Moestrup Ø2    Rehnstam-Holm, A.-S.3
  • 41
    • 0022260427 scopus 로고
    • Diffusion of extracellular hydrogen peroxide into intracellular compartments of human neutrophils. Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide
    • Ohno Y.G., Gallin J.I. Diffusion of extracellular hydrogen peroxide into intracellular compartments of human neutrophils. Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide. J. Biol. Chem. 260:1985;843-846.
    • (1985) J. Biol. Chem. , vol.260 , pp. 843-846
    • Ohno, Y.G.1    Gallin, J.I.2
  • 42
    • 0035286466 scopus 로고    scopus 로고
    • Specific growth rate plays a critical role in hydrogen peroxide resistance of the marine oligotrophic ultramicrobacterium Sphingomonas alaskensis strain RB2256
    • Ostrowski M., Cavicchioli R., Blaauw M., Gottschal J.C. Specific growth rate plays a critical role in hydrogen peroxide resistance of the marine oligotrophic ultramicrobacterium Sphingomonas alaskensis strain RB2256. Appl. Environ. Microbiol. 67:2001;1292-1299.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1292-1299
    • Ostrowski, M.1    Cavicchioli, R.2    Blaauw, M.3    Gottschal, J.C.4
  • 43
    • 0002835068 scopus 로고    scopus 로고
    • The structure of Perkinsus marinus (Mackin et al., 1950) Levine (1978) with comments on taxonomy and phylogeny of Perkinsus spp
    • Perkins F.O. The structure of Perkinsus marinus (Mackin et al., 1950) Levine (1978) with comments on taxonomy and phylogeny of Perkinsus spp. J. Shellfish Res. 15:1996;67-87.
    • (1996) J. Shellfish Res. , vol.15 , pp. 67-87
    • Perkins, F.O.1
  • 44
    • 0000809380 scopus 로고
    • Ultrastructure of sporulation in the oyster pathogen Dermocystidinuim marinum
    • Perkins F.O., Menzel R.W. Ultrastructure of sporulation in the oyster pathogen Dermocystidinuim marinum. J. Invertebr. Pathol. 9:1967;205-229.
    • (1967) J. Invertebr. Pathol. , vol.9 , pp. 205-229
    • Perkins, F.O.1    Menzel, R.W.2
  • 45
    • 0013866506 scopus 로고
    • Membrane properties of living mammalian cells as studied by enzymatic hydrolysis of fluorogenic esters
    • Rotman B., Papermaster B.W. Membrane properties of living mammalian cells as studied by enzymatic hydrolysis of fluorogenic esters. Proc. Natl. Acad. Sci. USA. 55:1966;134-141.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 134-141
    • Rotman, B.1    Papermaster, B.W.2
  • 46
    • 0034874061 scopus 로고    scopus 로고
    • Dinoflagellate nuclear SSU rRNA phylogeny suggests multiple plastid losses and replacements
    • Saldarriaga J., Taylor F., Keeling P., Cavalier-Smith T. Dinoflagellate nuclear SSU rRNA phylogeny suggests multiple plastid losses and replacements. J. Mol. Evol. 53:2001;204-213.
    • (2001) J. Mol. Evol. , vol.53 , pp. 204-213
    • Saldarriaga, J.1    Taylor, F.2    Keeling, P.3    Cavalier-Smith, T.4
  • 47
    • 0037237750 scopus 로고    scopus 로고
    • The PmSOD1 gene of the protistan parasite Perkinsus marinus complements the sod2Δ mutant of Saccharomyces cerevisiae, and directs an iron superoxide dismutase to mitochondria
    • Schott E.J., Vasta G.R. The PmSOD1 gene of the protistan parasite Perkinsus marinus complements the sod2Δ mutant of Saccharomyces cerevisiae, and directs an iron superoxide dismutase to mitochondria. Mol. Biochem. Parasitol. 126:2003;81-92.
    • (2003) Mol. Biochem. Parasitol. , vol.126 , pp. 81-92
    • Schott, E.J.1    Vasta, G.R.2
  • 48
    • 0022829302 scopus 로고
    • A comparison of leukocyte ascorbate levels measured by the 2,4-dinitrophenylhydrazine method with high-performance liquid chromatography
    • Schaus E.E., Kutnink M.A., O'Connor D.K., Omaye S. A comparison of leukocyte ascorbate levels measured by the 2,4-dinitrophenylhydrazine method with high-performance liquid chromatography. Biochem. Med. Metab. Biol. 36:1986;369-376.
    • (1986) Biochem. Med. Metab. Biol. , vol.36 , pp. 369-376
    • Schaus, E.E.1    Kutnink, M.A.2    O'Connor, D.K.3    Omaye, S.4
  • 49
    • 0030797866 scopus 로고    scopus 로고
    • Total evidence refutes the inclusion of Perkinsus species in the phylum Apicomplexa
    • Siddal M.E., Reece K.S., Graves J.E., Burreson E.M. Total evidence refutes the inclusion of Perkinsus species in the phylum Apicomplexa. Parasitology. 155:1997;165-176.
    • (1997) Parasitology , vol.155 , pp. 165-176
    • Siddal, M.E.1    Reece, K.S.2    Graves, J.E.3    Burreson, E.M.4
  • 50
    • 6144251157 scopus 로고    scopus 로고
    • NADPH oxidase-like activity in hemocytes of the Pacific oyster Crassostrea gigas
    • Takahashi K., Mori K. NADPH oxidase-like activity in hemocytes of the Pacific oyster Crassostrea gigas. Fish Pathol. 35:2000;15-19.
    • (2000) Fish Pathol. , vol.35 , pp. 15-19
    • Takahashi, K.1    Mori, K.2
  • 51
    • 0034697387 scopus 로고    scopus 로고
    • Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-1 to produce a soluble formazan: A simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents
    • Tan A.S., Berridge M.V. Superoxide produced by activated neutrophils efficiently reduces the tetrazolium salt, WST-1 to produce a soluble formazan: a simple colorimetric assay for measuring respiratory burst activation and for screening anti-inflammatory agents. J. Immunol. Methods. 238:2000;59-68.
    • (2000) J. Immunol. Methods , vol.238 , pp. 59-68
    • Tan, A.S.1    Berridge, M.V.2
  • 52
    • 0035849676 scopus 로고    scopus 로고
    • Unusual adaptive, cross protection responses and growth phase resistance against peroxide killing in a bacterial shrimp pathogen, Vibrio harveyi
    • Vattanaviboon P., Mongkolsuk S. Unusual adaptive, cross protection responses and growth phase resistance against peroxide killing in a bacterial shrimp pathogen, Vibrio harveyi. FEMS Microbiol. Lett. 200:2001;111-116.
    • (2001) FEMS Microbiol. Lett. , vol.200 , pp. 111-116
    • Vattanaviboon, P.1    Mongkolsuk, S.2
  • 53
    • 0024357032 scopus 로고
    • Role of hypochlorous acid in Trypanosoma musculi killing by phagocytes
    • Vincendeau P., Daulouede S., Veyret B. Role of hypochlorous acid in Trypanosoma musculi killing by phagocytes. Parasitology. 98(Part 2):1989;253-257.
    • (1989) Parasitology , vol.98 , Issue.PART 2 , pp. 253-257
    • Vincendeau, P.1    Daulouede, S.2    Veyret, B.3
  • 55
    • 0029025128 scopus 로고
    • Suppression of chemiluminescence of eastern oyster (Crassostrea virginica) hemocytes by the protozoan parasite Perkinsus marinus
    • Volety A.K., Chu F.L. Suppression of chemiluminescence of eastern oyster (Crassostrea virginica) hemocytes by the protozoan parasite Perkinsus marinus. Dev. Comp. Immunol. 19:1995;135-142.
    • (1995) Dev. Comp. Immunol. , vol.19 , pp. 135-142
    • Volety, A.K.1    Chu, F.L.2
  • 56
    • 0016382328 scopus 로고
    • Entamoeba histolytica. I. Aerobic metabolism
    • Weinbach E.C., Diamond L.S. Entamoeba histolytica. I. Aerobic metabolism. Exp. Parasitol. 35:1974;232-243.
    • (1974) Exp. Parasitol. , vol.35 , pp. 232-243
    • Weinbach, E.C.1    Diamond, L.S.2
  • 57
    • 0037053395 scopus 로고    scopus 로고
    • The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin
    • Wilkinson S.R., Meyer D.J., Taylor M.C., Bromley E.V., Miles M.A., Kelly J.M. The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin. J. Biol. Chem. 277:2002;17062-17071.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17062-17071
    • Wilkinson, S.R.1    Meyer, D.J.2    Taylor, M.C.3    Bromley, E.V.4    Miles, M.A.5    Kelly, J.M.6
  • 58
    • 0037036622 scopus 로고    scopus 로고
    • CDNA cloning and characterization of two iron superoxide dismutases from the oyster pathogen Perkinsus marinus
    • Wright A., Ahmed H., Gauthier J., Silva A., Vasta G. cDNA cloning and characterization of two iron superoxide dismutases from the oyster pathogen Perkinsus marinus. Mol. Biochem. Parasitol. 123:2002;73-77.
    • (2002) Mol. Biochem. Parasitol. , vol.123 , pp. 73-77
    • Wright, A.1    Ahmed, H.2    Gauthier, J.3    Silva, A.4    Vasta, G.5
  • 59
    • 0034063020 scopus 로고    scopus 로고
    • Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T) exhibiting high catalase activity
    • Yumoto I., Ichihashi D., Iwata H., Istokovics A., Ichise N., Matsuyama H., Okuyama H., Kawasaki K. Purification and characterization of a catalase from the facultatively psychrophilic bacterium Vibrio rumoiensis S-1(T) exhibiting high catalase activity. J. Bacteriol. 182:2000;1903-1909.
    • (2000) J. Bacteriol. , vol.182 , pp. 1903-1909
    • Yumoto, I.1    Ichihashi, D.2    Iwata, H.3    Istokovics, A.4    Ichise, N.5    Matsuyama, H.6    Okuyama, H.7    Kawasaki, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.