메뉴 건너뛰기




Volumn 159, Issue 3, 2006, Pages 196-204

Acetaldehyde does not inhibit glutathione peroxidase and glutathione reductase from mouse liver in vitro

Author keywords

Acetaldehyde; Ebselen; Ethanol; Glutathione peroxidase; Glutathione reductase; Glutamyltranspeptidase

Indexed keywords

ACETALDEHYDE; DITHIOERYTHRITOL; EBSELEN; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE;

EID: 84984586707     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2005.11.006     Document Type: Article
Times cited : (2)

References (58)
  • 1
    • 16644395874 scopus 로고    scopus 로고
    • Alcohol and thermally oxidized pufa induced oxidative stress: Role of N-acetyl cysteine
    • P.S. Varma, K. Aruna, R. Rukkumani, and V.P. Menon Alcohol and thermally oxidized pufa induced oxidative stress: role of N-acetyl cysteine Ital. J. Biochem. 53 2004 10 15
    • (2004) Ital. J. Biochem. , vol.53 , pp. 10-15
    • Varma, P.S.1    Aruna, K.2    Rukkumani, R.3    Menon, V.P.4
  • 2
    • 19544378737 scopus 로고    scopus 로고
    • Formation of acetaldehyde adducts of glutathione S-transferase A3 in the liver of rats administered alcohol chronically
    • R. Sultana, B.S. Raju, V. Sharma, P. Reddanna, and P.P. Babu Formation of acetaldehyde adducts of glutathione S-transferase A3 in the liver of rats administered alcohol chronically Alcohol 35 2005 57 66
    • (2005) Alcohol , vol.35 , pp. 57-66
    • Sultana, R.1    Raju, B.S.2    Sharma, V.3    Reddanna, P.4    Babu, P.P.5
  • 3
    • 0023543188 scopus 로고
    • Antibodies against acetaldehyde-modified protein epitopes in human alcoholics
    • O. Niemela, F. Klajner, H. Orrego, E. Vidins, L. Blendis, and Y. Israel Antibodies against acetaldehyde-modified protein epitopes in human alcoholics Hepatology 7 1987 1210 1214
    • (1987) Hepatology , vol.7 , pp. 1210-1214
    • Niemela, O.1    Klajner, F.2    Orrego, H.3    Vidins, E.4    Blendis, L.5    Israel, Y.6
  • 4
    • 0023860256 scopus 로고
    • Detection of a protein-acetaldehyde adduct in the liver of rats fed alcohol chronically
    • R.C. Lin, R.S. Smith, and L. Lumeng Detection of a protein-acetaldehyde adduct in the liver of rats fed alcohol chronically J. Clin. Invest. 81 1988 615 619
    • (1988) J. Clin. Invest. , vol.81 , pp. 615-619
    • Lin, R.C.1    Smith, R.S.2    Lumeng, L.3
  • 5
    • 0031416803 scopus 로고    scopus 로고
    • Detection of DNA adducts of acetaldehyde in peripheral white blood cells of alcohol abusers
    • J.L. Fang, and C.E. Vaca Detection of DNA adducts of acetaldehyde in peripheral white blood cells of alcohol abusers Carcinogenesis 18 1997 627 632
    • (1997) Carcinogenesis , vol.18 , pp. 627-632
    • Fang, J.L.1    Vaca, C.E.2
  • 6
    • 7044269393 scopus 로고    scopus 로고
    • Antioxidant properties of black tea in alcohol intoxication
    • W. Luczaj, and E. Skrzydlewska Antioxidant properties of black tea in alcohol intoxication Food Chem. Toxicol. 42 2004 2045 2051
    • (2004) Food Chem. Toxicol. , vol.42 , pp. 2045-2051
    • Luczaj, W.1    Skrzydlewska, E.2
  • 7
    • 1842428698 scopus 로고    scopus 로고
    • Green tea protects against ethanol-induced lipid peroxidation in rat organs
    • J. Ostrowska, W. Luczaj, I. Kasacka, A. Rozanski, and E. Skrzydlewska Green tea protects against ethanol-induced lipid peroxidation in rat organs Alcohol 32 2004 25 32
    • (2004) Alcohol , vol.32 , pp. 25-32
    • Ostrowska, J.1    Luczaj, W.2    Kasacka, I.3    Rozanski, A.4    Skrzydlewska, E.5
  • 8
    • 8644293199 scopus 로고    scopus 로고
    • Protective effects of taurine on glutathione and glutathione-dependent enzymes in ethanol-fed rats
    • G. Pushpakiran, K. Mahalakshmi, and C.V. Anuradha Protective effects of taurine on glutathione and glutathione-dependent enzymes in ethanol-fed rats Pharmazie 59 2004 869 872
    • (2004) Pharmazie , vol.59 , pp. 869-872
    • Pushpakiran, G.1    Mahalakshmi, K.2    Anuradha, C.V.3
  • 9
    • 0015226084 scopus 로고
    • Glutathione peroxidase: Enzymology and biological aspects
    • L. Flohe Glutathione peroxidase: enzymology and biological aspects Klin. Wochenschr. 49 1971 669 683
    • (1971) Klin. Wochenschr. , vol.49 , pp. 669-683
    • Flohe, L.1
  • 10
    • 0023242350 scopus 로고
    • The role of selenium peroxidases in the protection against oxidative damage of membranes
    • F. Ursini, and A. Bindoli The role of selenium peroxidases in the protection against oxidative damage of membranes Chem. Phys. Lipids 44 1987 255 276
    • (1987) Chem. Phys. Lipids , vol.44 , pp. 255-276
    • Ursini, F.1    Bindoli, A.2
  • 11
    • 0031659724 scopus 로고    scopus 로고
    • Influence of aminoguanidine on parameters of liver injury and regeneration induced in rats by a necrogenic dose of thioacetamide
    • C. Diez-Fernandez, N. Sanz, A.M. Alvarez, A. Zaragoza, and M. Cascales Influence of aminoguanidine on parameters of liver injury and regeneration induced in rats by a necrogenic dose of thioacetamide Br. J. Pharmacol. 125 1998 102 108
    • (1998) Br. J. Pharmacol. , vol.125 , pp. 102-108
    • Diez-Fernandez, C.1    Sanz, N.2    Alvarez, A.M.3    Zaragoza, A.4    Cascales, M.5
  • 12
    • 0036005658 scopus 로고    scopus 로고
    • Level of superoxide dismutase, glutathione peroxidase and uric acid in thioacetamide-induced cirrhotic rats
    • H. Abul, T.C. Mathew, H.M. Dashti, and A. Al-Bader Level of superoxide dismutase, glutathione peroxidase and uric acid in thioacetamide-induced cirrhotic rats Anat. Histol. Embryol. 31 2002 66 71
    • (2002) Anat. Histol. Embryol. , vol.31 , pp. 66-71
    • Abul, H.1    Mathew, T.C.2    Dashti, H.M.3    Al-Bader, A.4
  • 13
    • 84984539021 scopus 로고    scopus 로고
    • Additive pro-oxidative effects of methylmercury and ebselen in liver from suckling rat pups
    • M. Farina, F.A. Soares, G. Zeni, D.O. Souza, and J.B. Rocha Additive pro-oxidative effects of methylmercury and ebselen in liver from suckling rat pups Toxicol. Lett. 146 2004 227 235
    • (2004) Toxicol. Lett. , vol.146 , pp. 227-235
    • Farina, M.1    Soares, F.A.2    Zeni, G.3    Souza, D.O.4    Rocha, J.B.5
  • 14
    • 0021185122 scopus 로고
    • A novel biologically active seleno-organic compound. Part I. Glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ 51 (ebselen)
    • A. Muller, E. Cadenas, P. Graf, and H. Sies A novel biologically active seleno-organic compound. Part I. Glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ 51 (ebselen) Biochem. Pharmacol. 33 1984 3235 3239
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3235-3239
    • Muller, A.1    Cadenas, E.2    Graf, P.3    Sies, H.4
  • 15
    • 84984538861 scopus 로고    scopus 로고
    • Methylmercury increases glutamate release from brain synaptosomes and glutamate uptake by cortical slices from suckling rat pups: Modulatory effect of ebselen
    • M. Farina, K.C. Dahm, F.D. Schwalm, A.M. Brusque, M.E. Frizzo, G. Zeni, D.O. Souza, and J.B. Rocha Methylmercury increases glutamate release from brain synaptosomes and glutamate uptake by cortical slices from suckling rat pups: modulatory effect of ebselen Toxicol. Sci. 73 2003 135 140
    • (2003) Toxicol. Sci. , vol.73 , pp. 135-140
    • Farina, M.1    Dahm, K.C.2    Schwalm, F.D.3    Brusque, A.M.4    Frizzo, M.E.5    Zeni, G.6    Souza, D.O.7    Rocha, J.B.8
  • 17
    • 84984583119 scopus 로고    scopus 로고
    • Organoselenium and organotellurium compounds: Toxicology and pharmacology
    • C.W. Nogueira, G. Zeni, and J.B. Rocha Organoselenium and organotellurium compounds: toxicology and pharmacology Chem. Rev. 104 2004 6255 6285
    • (2004) Chem. Rev. , vol.104 , pp. 6255-6285
    • Nogueira, C.W.1    Zeni, G.2    Rocha, J.B.3
  • 18
    • 0031039324 scopus 로고    scopus 로고
    • Ebselen a novel anti-oxidant compound, protects the rat liver from ischemia-reperfusion injury
    • M. Ozaki, M. Nakamura, S. Teraoka, and K. Ota Ebselen a novel anti-oxidant compound, protects the rat liver from ischemia-reperfusion injury Transplant Int. 10 1997 96 102
    • (1997) Transplant Int. , vol.10 , pp. 96-102
    • Ozaki, M.1    Nakamura, M.2    Teraoka, S.3    Ota, K.4
  • 20
    • 0023891447 scopus 로고
    • Kinetic mechanism and substrate specificity of glutathione peroxidase activity of ebselen (PZ51)
    • M. Maiorino, A. Roveri, M. Coassin, and F. Ursini Kinetic mechanism and substrate specificity of glutathione peroxidase activity of ebselen (PZ51) Biochem. Pharmacol. 37 1988 2267 2271
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 2267-2271
    • Maiorino, M.1    Roveri, A.2    Coassin, M.3    Ursini, F.4
  • 21
    • 0022903803 scopus 로고
    • Synthetic seleno-organic compound with glutathione peroxidase-like activity in the chick
    • S.D. Mercurio, and G.F. Combs Jr. Synthetic seleno-organic compound with glutathione peroxidase-like activity in the chick Biochem. Pharmacol. 35 1986 4505 4509
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 4505-4509
    • Mercurio, S.D.1    Combs Jr., G.F.2
  • 23
    • 0037300963 scopus 로고    scopus 로고
    • Inhibition of glutathione reductase by cadmium ion in some rabbit tissues and the protective role of dietary selenium
    • N. Ulusu, N. Acan, B. Turan, and E. Tezcan Inhibition of glutathione reductase by cadmium ion in some rabbit tissues and the protective role of dietary selenium Biol. Trace Elem. Res. 91 2003 151 156
    • (2003) Biol. Trace Elem. Res. , vol.91 , pp. 151-156
    • Ulusu, N.1    Acan, N.2    Turan, B.3    Tezcan, E.4
  • 25
    • 0020521199 scopus 로고
    • The role of thiols in cellular response to radiation and drugs
    • J.E. Biaglow, M.E. Varnes, E.P. Clark, and E.R. Epp The role of thiols in cellular response to radiation and drugs Radiat. Res. 95 1983 437 455
    • (1983) Radiat. Res. , vol.95 , pp. 437-455
    • Biaglow, J.E.1    Varnes, M.E.2    Clark, E.P.3    Epp, E.R.4
  • 26
    • 0027569155 scopus 로고
    • Ameliorative capacities of vitamins and monothiols administered alone or in combinations in methylmercury mobilisation in nervous and non-nervous tissues of mice
    • P.P. Sood, K. Vijayalakshmi, and C. Bapu Ameliorative capacities of vitamins and monothiols administered alone or in combinations in methylmercury mobilisation in nervous and non-nervous tissues of mice Cell. Mol. Biol. (Noisy-le-grand) 39 1993 213 219
    • (1993) Cell. Mol. Biol. (Noisy-le-grand) , vol.39 , pp. 213-219
    • Sood, P.P.1    Vijayalakshmi, K.2    Bapu, C.3
  • 27
    • 1842409036 scopus 로고    scopus 로고
    • Role of oxidative stress and antioxidant therapy in alcoholic and nonalcoholic liver diseases
    • C.S. Lieber Role of oxidative stress and antioxidant therapy in alcoholic and nonalcoholic liver diseases Adv. Pharmacol. 38 1997 601 628
    • (1997) Adv. Pharmacol. , vol.38 , pp. 601-628
    • Lieber, C.S.1
  • 30
    • 0021369331 scopus 로고
    • Depression of biliary glutathione excretion by chronic ethanol feeding in the rat
    • G. Vendemiale, E. Jayatilleke, S. Shaw, and C.S. Lieber Depression of biliary glutathione excretion by chronic ethanol feeding in the rat Life Sci. 34 1984 1065 1073
    • (1984) Life Sci. , vol.34 , pp. 1065-1073
    • Vendemiale, G.1    Jayatilleke, E.2    Shaw, S.3    Lieber, C.S.4
  • 31
    • 0024412233 scopus 로고
    • Expedient synthesis of ebselen and related-compounds
    • L. Engman, and A. Hallberg Expedient synthesis of ebselen and related-compounds J. Org. Chem. 54 1989 2964 2966
    • (1989) J. Org. Chem. , vol.54 , pp. 2964-2966
    • Engman, L.1    Hallberg, A.2
  • 33
    • 0019740344 scopus 로고
    • Glutathione peroxidase
    • A. Wendel Glutathione peroxidase Meth. Enzymol. 77 1981 325 333
    • (1981) Meth. Enzymol. , vol.77 , pp. 325-333
    • Wendel, A.1
  • 34
    • 33845182896 scopus 로고
    • Development of synthetic compounds with glutathione peroxidase activity
    • S.R. Wlison, P.A. Zucker, R.C. Huang, and A. Spector Development of synthetic compounds with glutathione peroxidase activity J. Am. Chem. Soc. 111 1989 5936 5939
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5936-5939
    • Wlison, S.R.1    Zucker, P.A.2    Huang, R.C.3    Spector, A.4
  • 36
    • 0020677642 scopus 로고
    • Human blood acetaldehyde levels: With improved methods, a clearer picture emerges
    • K.O. Lindros Human blood acetaldehyde levels: with improved methods, a clearer picture emerges Alcohol. Clin. Exp. Res. 7 1983 70 75
    • (1983) Alcohol. Clin. Exp. Res. , vol.7 , pp. 70-75
    • Lindros, K.O.1
  • 37
    • 0021243586 scopus 로고
    • Blood and liver acetaldehyde concentrations during ethanol oxidation in C57 and DBA mice
    • C.J. Eriksson, N. Atkinson, D.R. Petersen, and R.A. Deitrich Blood and liver acetaldehyde concentrations during ethanol oxidation in C57 and DBA mice Biochem. Pharmacol. 33 1984 2213 2216
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 2213-2216
    • Eriksson, C.J.1    Atkinson, N.2    Petersen, D.R.3    Deitrich, R.A.4
  • 40
    • 0026640860 scopus 로고
    • Characterisation and quantitation of a selenol intermediate in the reaction of ebselen with thiols
    • I.A. Cotgreave, R. Morgenstern, L. Engman, and J. Ahokas Characterisation and quantitation of a selenol intermediate in the reaction of ebselen with thiols Chem. Biol. Interact. 84 1992 69 76
    • (1992) Chem. Biol. Interact. , vol.84 , pp. 69-76
    • Cotgreave, I.A.1    Morgenstern, R.2    Engman, L.3    Ahokas, J.4
  • 41
    • 12344265911 scopus 로고    scopus 로고
    • Glutathione metabolism is impaired in vitro by thallium(III) hydroxide
    • C.E. Hanzel, M.S. Villaverde, and S.V. Verstraeten Glutathione metabolism is impaired in vitro by thallium(III) hydroxide Toxicology 207 2005 501 510
    • (2005) Toxicology , vol.207 , pp. 501-510
    • Hanzel, C.E.1    Villaverde, M.S.2    Verstraeten, S.V.3
  • 42
    • 0037131424 scopus 로고    scopus 로고
    • A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase
    • R. Zhao, and A. Holmgren A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase J. Biol. Chem. 277 2002 39456 39462
    • (2002) J. Biol. Chem. , vol.277 , pp. 39456-39462
    • Zhao, R.1    Holmgren, A.2
  • 44
    • 0027240611 scopus 로고
    • Herman Award Lecture, 1993: A personal perspective on alcohol, nutrition, and the liver
    • C.S. Lieber Herman Award Lecture, 1993: a personal perspective on alcohol, nutrition, and the liver Am. J. Clin. Nutr. 58 1993 430 442
    • (1993) Am. J. Clin. Nutr. , vol.58 , pp. 430-442
    • Lieber, C.S.1
  • 45
    • 0021224125 scopus 로고
    • Increased microsomal oxidation of ethanol by cytochrome P-450 and hydroxyl radical-dependent pathways after chronic ethanol consumption
    • G. Krikun, C.S. Lieber, and A.I. Cederbaum Increased microsomal oxidation of ethanol by cytochrome P-450 and hydroxyl radical-dependent pathways after chronic ethanol consumption Biochem. Pharmacol. 33 1984 3306 3309
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3306-3309
    • Krikun, G.1    Lieber, C.S.2    Cederbaum, A.I.3
  • 46
    • 0020188453 scopus 로고
    • Oxidase and oxygenase function of the microsomal cytochrome P-450 monoxygenase system
    • H. Kuthan, and V. Ulbrich Oxidase and oxygenase function of the microsomal cytochrome P-450 monoxygenase system Eur. J. Biochem. 126 1982 583 588
    • (1982) Eur. J. Biochem. , vol.126 , pp. 583-588
    • Kuthan, H.1    Ulbrich, V.2
  • 47
    • 0023911853 scopus 로고
    • Spin trapping of free radical species produced during the microsomal metabolism of ethanol
    • E. Albano, A. Tomasi, L. Goria-Gatti, and M.U. Dianzani Spin trapping of free radical species produced during the microsomal metabolism of ethanol Chem. Biol. Interact. 65 1988 223 234
    • (1988) Chem. Biol. Interact. , vol.65 , pp. 223-234
    • Albano, E.1    Tomasi, A.2    Goria-Gatti, L.3    Dianzani, M.U.4
  • 48
    • 0027218413 scopus 로고
    • Increased NADPH- and NADH-dependent production of superoxide and hydroxyl radical by microsomes after chronic ethanol treatment
    • J. Rashba-Step, N.J. Turro, and A.I. Cederbaum Increased NADPH- and NADH-dependent production of superoxide and hydroxyl radical by microsomes after chronic ethanol treatment Arch. Biochem. Biophys. 300 1993 401 408
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 401-408
    • Rashba-Step, J.1    Turro, N.J.2    Cederbaum, A.I.3
  • 49
    • 0028016469 scopus 로고
    • Ethanol treatment up-regulates the expression of mitochondrial manganese superoxide dismutase in rat liver
    • O.R. Koch, M.E. De Leo, S. Borrello, G. Palombini, and T. Galeotti Ethanol treatment up-regulates the expression of mitochondrial manganese superoxide dismutase in rat liver Biochem. Biophys. Res. Commun. 201 1994 1356 1365
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 1356-1365
    • Koch, O.R.1    De Leo, M.E.2    Borrello, S.3    Palombini, G.4    Galeotti, T.5
  • 50
    • 0028897706 scopus 로고
    • Effect of type of dietary fat and ethanol on antioxidant enzyme mRNA induction in rat liver
    • A.A. Nanji, B. Griniuviene, S.M. Sadrzadeh, S. Levitsky, and J.D. McCully Effect of type of dietary fat and ethanol on antioxidant enzyme mRNA induction in rat liver J. Lipid Res. 36 1995 736 744
    • (1995) J. Lipid Res. , vol.36 , pp. 736-744
    • Nanji, A.A.1    Griniuviene, B.2    Sadrzadeh, S.M.3    Levitsky, S.4    McCully, J.D.5
  • 51
    • 0031979979 scopus 로고    scopus 로고
    • Increased lipid peroxidation and impaired antioxidant enzyme function is associated with pathological liver injury in experimental alcoholic liver disease in rats fed diets high in corn oil and fish oil
    • R. Polavarapu, D.R. Spitz, J.E. Sim, M.H. Follansbee, L.W. Oberley, A. Rahemtulla, and A.A. Nanji Increased lipid peroxidation and impaired antioxidant enzyme function is associated with pathological liver injury in experimental alcoholic liver disease in rats fed diets high in corn oil and fish oil Hepatology 27 1998 1317 1323
    • (1998) Hepatology , vol.27 , pp. 1317-1323
    • Polavarapu, R.1    Spitz, D.R.2    Sim, J.E.3    Follansbee, M.H.4    Oberley, L.W.5    Rahemtulla, A.6    Nanji, A.A.7
  • 52
    • 0035026194 scopus 로고    scopus 로고
    • Chronic ethanol consumption alters the glutathione/glutathione peroxidase-1 system and protein oxidation status in rat liver
    • S.M. Bailey, V.B. Patel, T.A. Young, K. Asayama, and C.C. Cunningham Chronic ethanol consumption alters the glutathione/glutathione peroxidase-1 system and protein oxidation status in rat liver Alcohol. Clin. Exp. Res. 25 2001 726 733
    • (2001) Alcohol. Clin. Exp. Res. , vol.25 , pp. 726-733
    • Bailey, S.M.1    Patel, V.B.2    Young, T.A.3    Asayama, K.4    Cunningham, C.C.5
  • 53
    • 0032955185 scopus 로고    scopus 로고
    • Glutathione S-transferases - A review
    • A.E. Salinas, and M.G. Wong Glutathione S-transferases - a review Curr. Med. Chem. 6 1999 279 309
    • (1999) Curr. Med. Chem. , vol.6 , pp. 279-309
    • Salinas, A.E.1    Wong, M.G.2
  • 54
    • 0036667842 scopus 로고    scopus 로고
    • 4-Hydroxynonenal detoxification by mitochondrial glutathione S-transferase is compromised by short-term ethanol consumption in rats
    • J. Chen, S. Schenker, and G.I. Henderson 4-Hydroxynonenal detoxification by mitochondrial glutathione S-transferase is compromised by short-term ethanol consumption in rats Alcohol. Clin. Exp. Res. 26 2002 1252 1258
    • (2002) Alcohol. Clin. Exp. Res. , vol.26 , pp. 1252-1258
    • Chen, J.1    Schenker, S.2    Henderson, G.I.3
  • 56
    • 0016913988 scopus 로고
    • Gamma-glutamyltranspeptidase (GGTP): Its relationship to other enzymes for diagnosis of liver disease
    • B. Dragosics, P. Ferenci, F. Pesendorfer, and F.G. Wewalka Gamma-glutamyltranspeptidase (GGTP): its relationship to other enzymes for diagnosis of liver disease Prog. Liver Dis. 5 1976 436 449
    • (1976) Prog. Liver Dis. , vol.5 , pp. 436-449
    • Dragosics, B.1    Ferenci, P.2    Pesendorfer, F.3    Wewalka, F.G.4
  • 57
    • 0022372974 scopus 로고
    • Conjugation of acetaldehyde with cysteinylglycine, the first metabolite in glutathione breakdown by gamma-glutamyltranspeptidase
    • Y. Kera, T. Kiriyama, and S. Komura Conjugation of acetaldehyde with cysteinylglycine, the first metabolite in glutathione breakdown by gamma-glutamyltranspeptidase Agents Actions 17 1985 48 52
    • (1985) Agents Actions , vol.17 , pp. 48-52
    • Kera, Y.1    Kiriyama, T.2    Komura, S.3
  • 58
    • 0142072095 scopus 로고    scopus 로고
    • Binding of acetaldehyde to a glutathione metabolite: Mass spectrometric characterization of an acetaldehyde-cysteinylglycine conjugate
    • H. Anni, P. Pristatsky, and Y. Israel Binding of acetaldehyde to a glutathione metabolite: mass spectrometric characterization of an acetaldehyde-cysteinylglycine conjugate Alcohol. Clin. Exp. Res. 27 2003 1613 1621
    • (2003) Alcohol. Clin. Exp. Res. , vol.27 , pp. 1613-1621
    • Anni, H.1    Pristatsky, P.2    Israel, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.