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Volumn 101, Issue 5, 2007, Pages 1373-1381

Characterization of Taenia solium cysticerci microsomal glutathione S-transferase activity

Author keywords

[No Author keywords available]

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; 1,2 DICHLORO 4 NITROBENZENE; 4 HYDROXYNONENAL; GLUCOSE 6 PHOSPHATASE; GLUTATHIONE TRANSFERASE; LACTATE DEHYDROGENASE; MUCONALDEHYDE; SUCCINATE DEHYDROGENASE;

EID: 34548594212     PISSN: 09320113     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00436-007-0655-z     Document Type: Article
Times cited : (9)

References (52)
  • 1
    • 0023834368 scopus 로고
    • Activation and inhibition of microsomal glutathione S-transferase from mouse liver
    • Anderson C, Soderstrom M, Mannervick B (1988) Activation and inhibition of microsomal glutathione S-transferase from mouse liver. Biochem J 249:819-823
    • (1988) Biochem J , vol.249 , pp. 819-823
    • Anderson, C.1    Soderstrom, M.2    Mannervick, B.3
  • 3
    • 0000522311 scopus 로고
    • Limitations of the phenazine methosulfate assay for succinic and related dehydrogenase
    • Arrigoni O, Singer TP (1962) Limitations of the phenazine methosulfate assay for succinic and related dehydrogenase. Nature (London) 193:1256-1258
    • (1962) Nature (London) , vol.193 , pp. 1256-1258
    • Arrigoni, O.1    Singer, T.P.2
  • 4
    • 0018289604 scopus 로고
    • Xenobiotic metabolizing enzymes in Drosophila melanogaster. Activities of epoxide hydratasa and glutathione S-transferase compared with similar activities in rat liver
    • Baars AJ, Jansen M, Breimer D (1979) Xenobiotic metabolizing enzymes in Drosophila melanogaster. Activities of epoxide hydratasa and glutathione S-transferase compared with similar activities in rat liver. Mutation Res 62:279-291
    • (1979) Mutation Res , vol.62 , pp. 279-291
    • Baars, A.J.1    Jansen, M.2    Breimer, D.3
  • 5
    • 0028787866 scopus 로고
    • Characterization of arachidonic-acid-metabolizing enzymes in adult Schistosoma mansoni
    • Baset HA, O'Neill GP, Ford-Hutchinson AW (1995) Characterization of arachidonic-acid-metabolizing enzymes in adult Schistosoma mansoni. Mol Biochem Parasitol 73:31-41
    • (1995) Mol Biochem Parasitol , vol.73 , pp. 31-41
    • Baset, H.A.1    O'Neill, G.P.2    Ford-Hutchinson, A.W.3
  • 6
    • 0029118391 scopus 로고
    • Eicosanoid production by parasites: From pathogenesis to immunomodulation?
    • Belley A, Chadee K (1995) Eicosanoid production by parasites: from pathogenesis to immunomodulation? Parasitol Today 11:327-334
    • (1995) Parasitol Today , vol.11 , pp. 327-334
    • Belley, A.1    Chadee, K.2
  • 8
    • 0024366016 scopus 로고
    • Glutathione transferases in the tapeworm Moniezia expansa
    • Brophy PM, Southan C, Barret J (1989) Glutathione transferases in the tapeworm Moniezia expansa. Biochem J 262:939-946
    • (1989) Biochem J , vol.262 , pp. 939-946
    • Brophy, P.M.1    Southan, C.2    Barret, J.3
  • 9
    • 0025330875 scopus 로고
    • Glutathione transferase in helminthes
    • Brophy PM, Barret J (1990) Glutathione transferase in helminthes. Parasitology 100:345-349
    • (1990) Parasitology , vol.100 , pp. 345-349
    • Brophy, P.M.1    Barret, J.2
  • 10
    • 0025873235 scopus 로고
    • LY178002 reduces rat brain damage after transient global forebrain ischemia
    • Clemens JA, Ho PP, Panetta JA (1991) LY178002 reduces rat brain damage after transient global forebrain ischemia. Stroke 22:1048-1052
    • (1991) Stroke , vol.22 , pp. 1048-1052
    • Clemens, J.A.1    Ho, P.P.2    Panetta, J.A.3
  • 11
    • 38249037914 scopus 로고
    • The genetics of xenobiotic metabolism in Drosophila. IV. Purification and characterization of the major glutathione S-transferase
    • Cochrane BJ, Morrissey JJ, LeBlanc GA (1987) The genetics of xenobiotic metabolism in Drosophila. IV. Purification and characterization of the major glutathione S-transferase. Insect Biochem 17:731-738
    • (1987) Insect Biochem , vol.17 , pp. 731-738
    • Cochrane, B.J.1    Morrissey, J.J.2    Leblanc, G.A.3
  • 12
    • 0021950853 scopus 로고
    • 4-hydroxyalk-2-enals are substrates for transferase
    • Danielson PUH, Mannervik B (1985) 4-hydroxyalk-2-enals are substrates for transferase. FEBS 179:267-270
    • (1985) FEBS , vol.179 , pp. 267-270
    • Danielson, P.U.H.1    Mannervik, B.2
  • 13
    • 77049229661 scopus 로고
    • Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue
    • deDuve C, Pressman BC, Gianetto R, Wattiaux R, Appelmans F (1955) Tissue fractionation studies. 6. Intracellular distribution patterns of enzymes in rat-liver tissue. Biochem J 60:604-617
    • (1955) Biochem J , vol.60 , pp. 604-617
    • Deduve, C.1    Pressman, B.C.2    Gianetto, R.3    Wattiaux, R.4    Appelmans, F.5
  • 14
    • 38249036465 scopus 로고
    • Soluble glutathione S-transferase isoenzymes in Daphnia magna strains and their interactions with 2,4-dichlorophenoxy acetic acid and 1,4-benzoquinone
    • Dierickx PJ (1987) Soluble glutathione S-transferase isoenzymes in Daphnia magna strains and their interactions with 2,4-dichlorophenoxy acetic acid and 1,4-benzoquinone. Insect Biochem 17:1-6
    • (1987) Insect Biochem , vol.17 , pp. 1-6
    • Dierickx, P.J.1
  • 17
    • 84988106922 scopus 로고
    • Enzyme-structure relationships in the endoplasmic reticulum of rat liver. a morphological and biochemical study
    • Ernster L, Siekevitz P, Palade G (1962) Enzyme-structure relationships in the endoplasmic reticulum of rat liver. A morphological and biochemical study. J Cell Biol 15:541-562
    • (1962) J Cell Biol , vol.15 , pp. 541-562
    • Ernster, L.1    Siekevitz, P.2    Palade, G.3
  • 19
    • 0000154206 scopus 로고
    • The colorimetric determination of phosphorus
    • Fiske CH, SubbaRow Y (1925) The colorimetric determination of phosphorus. J Biol Chem 66:375-400
    • (1925) J Biol Chem , vol.66 , pp. 375-400
    • Fiske, C.H.1    Subbarow, Y.2
  • 21
    • 0018787711 scopus 로고
    • The identification, solubilization, and characterization of microsome-associated glutathione S-transferases
    • Friedberg T, Bentley Ph, Stasiecki P, Glatt HR, Raphael D, Oesch F (1979) The identification, solubilization, and characterization of microsome-associated glutathione S-transferases. J Biol Chem 254:12028-12033
    • (1979) J Biol Chem , vol.254 , pp. 12028-12033
    • Friedberg, T.1    Ph, B.2    Stasiecki, P.3    Glatt, H.R.4    Raphael, D.5    Oesch, F.6
  • 22
    • 0022498795 scopus 로고
    • Schistosoma mansoni: Production of cercarial eicosanoids as correlates of penetration and transformation
    • Fusco AC, Salafsky B, Delbrook K (1986) Schistosoma mansoni. : production of cercarial eicosanoids as correlates of penetration and transformation. J Parasitol 72:397-404
    • (1986) J Parasitol , vol.72 , pp. 397-404
    • Fusco, A.C.1    Salafsky, B.2    Delbrook, K.3
  • 23
    • 0036042282 scopus 로고    scopus 로고
    • Purification of Taenia solium cysticerci superoxide dismutase and myoglobin copurification
    • Gonzalez R, Mendoza-Hernandez G, Plancarte A (2002) Purification of Taenia solium cysticerci superoxide dismutase and myoglobin copurification. Parasitol Res 88:881-887
    • (2002) Parasitol Res , vol.88 , pp. 881-887
    • Gonzalez, R.1    Mendoza-Hernandez, G.2    Plancarte, A.3
  • 24
    • 0016275313 scopus 로고
    • Glutathione S-transferase. the first enzymatic step in mercapturic acid formation
    • Habig WH, Pabst MJ, Jakoby WB (1974) Glutathione S-transferase. The first enzymatic step in mercapturic acid formation. J Biol Chem 249:7130-7139
    • (1974) J Biol Chem , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 25
  • 26
    • 0017911441 scopus 로고
    • The glutathione S-transferases: A group of multifunctional detoxification proteins
    • Jakoby WB (1978) The glutathione S-transferases: a group of multifunctional detoxification proteins. Adv Enzymol 46:383-414
    • (1978) Adv Enzymol , vol.46 , pp. 383-414
    • Jakoby, W.B.1
  • 29
    • 0020644860 scopus 로고
    • 2 generation and release by the larvae stage of the cestode, Taenia taeniaeformis
    • 2 generation and release by the larvae stage of the cestode, Taenia taeniaeformis. Prostaglandins Leukot Med 11:317-323
    • (1983) Prostaglandins Leukot Med , vol.11 , pp. 317-323
    • Leid, R.W.1    McConnell, L.A.2
  • 30
    • 0023275606 scopus 로고
    • Parasite defense mechanism for evasion of host attack: A review
    • Leid RW, Suquet CM, Taniagoshi L (1987) Parasite defense mechanism for evasion of host attack: a review. Vet Parasitol 25:147-162
    • (1987) Vet Parasitol , vol.25 , pp. 147-162
    • Leid, R.W.1    Suquet, C.M.2    Taniagoshi, L.3
  • 31
    • 0021104760 scopus 로고
    • Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition
    • Morgenstern R, DePierre W (1983) Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition. Eur J Biochem 134:591-597
    • (1983) Eur J Biochem , vol.134 , pp. 591-597
    • Morgenstern, R.1    DePierre, W.2
  • 32
    • 0018789315 scopus 로고
    • Activation of microsomal glutathione S-transfrease activity by sulfhydryl reagents
    • Morgenstern R, DePierre JW, Ernster L (1979) Activation of microsomal glutathione S-transfrease activity by sulfhydryl reagents. Biochem Biophys Res Commun 87:657-663
    • (1979) Biochem Biophys Res Commun , vol.87 , pp. 657-663
    • Morgenstern, R.1    Depierre, J.W.2    Ernster, L.3
  • 33
    • 0018979047 scopus 로고
    • Characterization of rat-liver microsomal glutathione S-transferase activity
    • Morgenstern R, Meijer J, DePierre JW, Ernster L (1980) Characterization of rat-liver microsomal glutathione S-transferase activity. Eur J Biochem 104:167-174
    • (1980) Eur J Biochem , vol.104 , pp. 167-174
    • Morgenstern, R.1    Meijer, J.2    Depierre, J.W.3    Ernster, L.4
  • 34
    • 0023915262 scopus 로고
    • Studies on the activity and activation of rat liver microsomal glutathione S-transferase, in particular with a substrate analogue series
    • Morgenstern R, Lundqvist G, Hancock V, DePierre W (1988) Studies on the activity and activation of rat liver microsomal glutathione S-transferase, in particular with a substrate analogue series. J Biol Chem 263:6671-6675
    • (1988) J Biol Chem , vol.263 , pp. 6671-6675
    • Morgenstern, R.1    Lundqvist, G.2    Hancock, V.3    Depierre, W.4
  • 35
    • 0024437208 scopus 로고
    • Activity of rat liver microsomal glutathione transferase toward products of lipid peroxidation and studies of the effect of inhibitors on glutathione-dependent protection against lipid peroxidation
    • Mosialou E, Morgenstern R (1989) Activity of rat liver microsomal glutathione transferase toward products of lipid peroxidation and studies of the effect of inhibitors on glutathione-dependent protection against lipid peroxidation. Arch Biochem Biophys 275:289-294
    • (1989) Arch Biochem Biophys , vol.275 , pp. 289-294
    • Mosialou, E.1    Morgenstern, R.2
  • 36
    • 0025250263 scopus 로고
    • Inhibition studies on rat liver microsomal glutathione transferase
    • Mosialou E, Morgenstern R (1990) Inhibition studies on rat liver microsomal glutathione transferase. Chem Biol Interact 74:275-280
    • (1990) Chem Biol Interact , vol.74 , pp. 275-280
    • Mosialou, E.1    Morgenstern, R.2
  • 38
    • 0026902170 scopus 로고
    • Schistosoma mansoni: Single step purification and characterization of glutathione S-transferase isoenzyme 4
    • O'Leary KA, Hathaway KM, Tracy JW (1992) Schistosoma mansoni. : single step purification and characterization of glutathione S-transferase isoenzyme 4. Exp Parasitol 75:47-55
    • (1992) Exp Parasitol , vol.75 , pp. 47-55
    • O'Leary, K.A.1    Hathaway, K.M.2    Tracy, J.W.3
  • 39
    • 0014108436 scopus 로고
    • Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase
    • Paglia DE, Valentine WN (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70:158-169
    • (1967) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 40
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson GL (1977) A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 83:346-356
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 41
    • 3042572702 scopus 로고    scopus 로고
    • Purification, characterization and kinetic properties of the Taenia solium glutathione S-transferase isoform 26.5 kDa
    • Plancarte A, Rendón JL, Landa A (2004) Purification, characterization and kinetic properties of the Taenia solium glutathione S-transferase isoform 26.5 kDa. Parasitol Res 93:137-144
    • (2004) Parasitol Res , vol.93 , pp. 137-144
    • Plancarte, A.1    Rendón, J.L.2    Landa, A.3
  • 46
    • 0014444144 scopus 로고
    • A low viscosity epoxy resin embedding medium for electron microscopy
    • Spurr AR (1969) A low viscosity epoxy resin embedding medium for electron microscopy. J Ultrastruct Res 26:31
    • (1969) J Ultrastruct Res , vol.26 , pp. 31
    • Spurr, A.R.1
  • 47
    • 77957006891 scopus 로고
    • Glucose-6-phosphatase from liver
    • Swanson MA (1955) Glucose-6-phosphatase from liver. Methods Enzymol 2:541-543
    • (1955) Methods Enzymol , vol.2 , pp. 541-543
    • Swanson, M.A.1
  • 48
    • 0021918821 scopus 로고
    • Inhibitors for distinction of three types of human glutathione transferase
    • Tahir MK, Mannervik B (1985) Inhibitors for distinction of three types of human glutathione transferase. FEBS Lett 181:249-252
    • (1985) FEBS Lett , vol.181 , pp. 249-252
    • Tahir, M.K.1    Mannervik, B.2
  • 49
    • 0022623382 scopus 로고
    • Simple inhibition studies for distinction between homodimeric and heterodimeric isoenzymes of glutathione transferase
    • Tahir MK, Mannervik B (1986) Simple inhibition studies for distinction between homodimeric and heterodimeric isoenzymes of glutathione transferase. J Biol Chem 261:1048-1051
    • (1986) J Biol Chem , vol.261 , pp. 1048-1051
    • Tahir, M.K.1    Mannervik, B.2
  • 51
    • 0036219856 scopus 로고    scopus 로고
    • Characterization of a recombinant mu-class glutathione S-transferase from Taenia solium
    • Vibanco-Perez N, Jiménez L, Mendoza-Hernandez G, Landa A (2002) Characterization of a recombinant mu-class glutathione S-transferase from Taenia solium. Parasitol Res 88:398-404
    • (2002) Parasitol Res , vol.88 , pp. 398-404
    • Vibanco-Perez, N.1    Jiménez, L.2    Mendoza-Hernandez, G.3    Landa, A.4


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