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Volumn 72, Issue 6, 1999, Pages 2523-2530

The glutathione system of peroxide detoxification is less efficient in neurons than in astroglial cells

Author keywords

Astrocytes; Cumene hydroperoxide; Glutathione; Hydrogen peroxide; Neurons; Oxidative stress

Indexed keywords

AMITROLE; CUMENE HYDROPEROXIDE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROGEN PEROXIDE;

EID: 0032974143     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0722523.x     Document Type: Article
Times cited : (203)

References (55)
  • 1
    • 0031839462 scopus 로고    scopus 로고
    • Characterization of t-butyl hydroperoxide toxicity in cultured rat cortical neurones and astrocytes
    • Abe K. and Saito H. (1998) Characterization of t-butyl hydroperoxide toxicity in cultured rat cortical neurones and astrocytes. Pharmacol. Toxicol. 83, 40-46.
    • (1998) Pharmacol. Toxicol. , vol.83 , pp. 40-46
    • Abe, K.1    Saito, H.2
  • 2
    • 0000024076 scopus 로고
    • Catalase
    • (Bergmeyer H. U., ed), Verlag Chemie, Weinheim, Germany
    • Aebi H. E. (1984) Catalase, in Methods of Enzymatic Analysis, Vol. 3 (Bergmeyer H. U., ed), pp. 273-286. Verlag Chemie, Weinheim, Germany.
    • (1984) Methods of Enzymatic Analysis , vol.3 , pp. 273-286
    • Aebi, H.E.1
  • 3
    • 0031418498 scopus 로고    scopus 로고
    • Neurodegenerative disorders in humans: The role of glutathione in oxidative stress-mediated neuronal death
    • Bains J. S. and Shaw C. A. (1997) Neurodegenerative disorders in humans: the role of glutathione in oxidative stress-mediated neuronal death. Brain Res. Rev. 25, 335-358.
    • (1997) Brain Res. Rev. , vol.25 , pp. 335-358
    • Bains, J.S.1    Shaw, C.A.2
  • 4
    • 0025043947 scopus 로고
    • Microtiter plate assay for the measurement of glutathione and glutathione disulfide in large numbers of biological samples
    • Baker M. A., Cerniglia G. J., and Zaman A. (1990) Microtiter plate assay for the measurement of glutathione and glutathione disulfide in large numbers of biological samples. Anal. Biochem. 190, 360-365.
    • (1990) Anal. Biochem. , vol.190 , pp. 360-365
    • Baker, M.A.1    Cerniglia, G.J.2    Zaman, A.3
  • 5
    • 0023763728 scopus 로고
    • Function and regulation of the pentose phosphate pathway in brain
    • Baquer N. Z., Hothersall J. S., and McLean P. (1988) Function and regulation of the pentose phosphate pathway in brain. Curr. Top. Cell. Regul. 29, 265-289.
    • (1988) Curr. Top. Cell. Regul. , vol.29 , pp. 265-289
    • Baquer, N.Z.1    Hothersall, J.S.2    McLean, P.3
  • 6
    • 0029962693 scopus 로고    scopus 로고
    • Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage: Implication for neuronal/astrocytic trafficking and neurodegeneration
    • Barker J. E., Bolaños J. P., Land J. M., Clark J. B., and Heales S. J. R. (1996) Glutathione protects astrocytes from peroxynitrite-mediated mitochondrial damage: implication for neuronal/astrocytic trafficking and neurodegeneration. Dev. Neurosci. 18, 391-396.
    • (1996) Dev. Neurosci. , vol.18 , pp. 391-396
    • Barker, J.E.1    Bolaños, J.P.2    Land, J.M.3    Clark, J.B.4    Heales, S.J.R.5
  • 7
    • 0028648281 scopus 로고
    • Oxidative stress in the central nervous system: Monitoring the metabolic response using the pentose phosphate pathway
    • Ben-Yoseph O., Boxer P. A., and Ross B. D. (1994) Oxidative stress in the central nervous system: monitoring the metabolic response using the pentose phosphate pathway. Dev. Neurosci. 16, 328-336.
    • (1994) Dev. Neurosci. , vol.16 , pp. 328-336
    • Ben-Yoseph, O.1    Boxer, P.A.2    Ross, B.D.3
  • 8
    • 0030008721 scopus 로고    scopus 로고
    • Assessment of the role of the glutathione and pentose phosphate pathways in the protection of primary cerebrocortical cultures from oxidative stress
    • Ben-Yoseph O., Boxer P. A., and Ross B. D. (1996) Assessment of the role of the glutathione and pentose phosphate pathways in the protection of primary cerebrocortical cultures from oxidative stress. J. Neurochem. 66, 2329-2337.
    • (1996) J. Neurochem. , vol.66 , pp. 2329-2337
    • Ben-Yoseph, O.1    Boxer, P.A.2    Ross, B.D.3
  • 9
    • 0028278638 scopus 로고
    • The functional role of monoamine oxidases A and B in the mammalian central nervous system
    • Berry M. D., Juorio A. V., and Paterson I. A. (1994) The functional role of monoamine oxidases A and B in the mammalian central nervous system. Prog. Neurobiol. 42, 375-391.
    • (1994) Prog. Neurobiol. , vol.42 , pp. 375-391
    • Berry, M.D.1    Juorio, A.V.2    Paterson, I.A.3
  • 10
    • 0027059107 scopus 로고
    • Eicosanoid formation in the rat cerebral cortex. Contribution of neurons and glia
    • Bishai I. and Coceani F. (1992) Eicosanoid formation in the rat cerebral cortex. Contribution of neurons and glia. Mol. Chem. Neuropathol. 17, 219-238.
    • (1992) Mol. Chem. Neuropathol. , vol.17 , pp. 219-238
    • Bishai, I.1    Coceani, F.2
  • 11
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolaños J. P., Heales S. J. R., Land J. M., and Clark J. B. (1995) Effect of peroxynitrite on the mitochondrial respiratory chain: differential susceptibility of neurones and astrocytes in primary culture. J. Neurochem. 64, 1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolaños, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 12
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling A. C. and Beal M. F. (1995) Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56, 1151-1171.
    • (1995) Life Sci. , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 13
    • 0031200869 scopus 로고    scopus 로고
    • Free radicals and the pathology of brain dopamine systems
    • Cadet J. L. and Brannock C. (1998) Free radicals and the pathology of brain dopamine systems. Neurochem. Int. 32, 117-131.
    • (1998) Neurochem. Int. , vol.32 , pp. 117-131
    • Cadet, J.L.1    Brannock, C.2
  • 14
    • 0002865475 scopus 로고    scopus 로고
    • Glutathione in the brain: Disorders of glutathione metabolism
    • (Rosenberg R. N., Prusiner S. B., DiMauro S., Barchi R. L., and Kunk L. M., eds), Butterworth-Heinemann, Boston
    • Cooper A. J. L. (1997) Glutathione in the brain: disorders of glutathione metabolism, in The Molecular and Genetic Basis of Neurological Disease (Rosenberg R. N., Prusiner S. B., DiMauro S., Barchi R. L., and Kunk L. M., eds), pp. 1195-1230. Butterworth-Heinemann, Boston.
    • (1997) The Molecular and Genetic Basis of Neurological Disease , pp. 1195-1230
    • Cooper, A.J.L.1
  • 16
    • 0029990439 scopus 로고    scopus 로고
    • Astrocytes protect neurons from hydrogen peroxide toxicity
    • Desagher S., Glowinski J., and Premont J. (1996) Astrocytes protect neurons from hydrogen peroxide toxicity. J. Neurosci. 16, 2553-2562.
    • (1996) J. Neurosci. , vol.16 , pp. 2553-2562
    • Desagher, S.1    Glowinski, J.2    Premont, J.3
  • 17
    • 0029836312 scopus 로고    scopus 로고
    • Glutathione content as an indicator for the presence of metabolic pathways of amino acids in astroglial cultures
    • Dringen R. and Hamprecht B. (1996) Glutathione content as an indicator for the presence of metabolic pathways of amino acids in astroglial cultures. J. Neurochem. 67, 1375-1382.
    • (1996) J. Neurochem. , vol.67 , pp. 1375-1382
    • Dringen, R.1    Hamprecht, B.2
  • 18
    • 0030852097 scopus 로고    scopus 로고
    • Involvement of glutathione peroxidase and catalase in the disposal of exogenous hydrogen peroxide by cultured astroglial cells
    • Dringen R. and Hamprecht B. (1997) Involvement of glutathione peroxidase and catalase in the disposal of exogenous hydrogen peroxide by cultured astroglial cells. Brain Res. 759, 67-75.
    • (1997) Brain Res. , vol.759 , pp. 67-75
    • Dringen, R.1    Hamprecht, B.2
  • 19
    • 0032104841 scopus 로고    scopus 로고
    • Rapid clearance of tertiary butyl hydroperoxide by cultured astroglial cells via oxidation of glutathione
    • Dringen R., Kussmaul L., and Hamprecht B. (1998a) Rapid clearance of tertiary butyl hydroperoxide by cultured astroglial cells via oxidation of glutathione. Glia 23, 139-145.
    • (1998) Glia , vol.23 , pp. 139-145
    • Dringen, R.1    Kussmaul, L.2    Hamprecht, B.3
  • 20
    • 0031808935 scopus 로고    scopus 로고
    • Detoxification of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by a microtiter plate assay
    • Dringen R., Kussmaul L., and Hamprecht B. (1998b) Detoxification of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by a microtiter plate assay. Brain Res. Protocols 2, 223-228.
    • (1998) Brain Res. Protocols , vol.2 , pp. 223-228
    • Dringen, R.1    Kussmaul, L.2    Hamprecht, B.3
  • 21
    • 0033555806 scopus 로고    scopus 로고
    • Synthesis of the antioxidant glutathione in neurons: Supply by astrocytes of CysGly as precursor for neuronal glutathione
    • Dringen R., Pfeiffer B., and Hamprecht B. (1999) Synthesis of the antioxidant glutathione in neurons: supply by astrocytes of CysGly as precursor for neuronal glutathione. J. Neurosci. 19, 562-569.
    • (1999) J. Neurosci. , vol.19 , pp. 562-569
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 22
    • 0021345735 scopus 로고
    • Oxidation of glutathione during hydroperoxide metabolism. A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2-chloroethyl)-1-nitrosourea
    • Eklöw L., Moldeus P., and Orrenius S. (1984) Oxidation of glutathione during hydroperoxide metabolism. A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2-chloroethyl)-1-nitrosourea. Eur. J. Biochem. 138, 459-463.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 459-463
    • Eklöw, L.1    Moldeus, P.2    Orrenius, S.3
  • 23
    • 0021288821 scopus 로고
    • Assays for glutathione peroxidase
    • Flohé L. and Günzler W. A. (1984) Assays for glutathione peroxidase. Methods Enzymol. 105, 114-121.
    • (1984) Methods Enzymol. , vol.105 , pp. 114-121
    • Flohé, L.1    Günzler, W.A.2
  • 24
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. (1995) Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64, 97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 25
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. (1992) Reactive oxygen species and the central nervous system. J. Neurochem. 59, 1609-1623.
    • (1992) J. Neurochem. , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 26
    • 0002200343 scopus 로고
    • Energy metabolism
    • (Kettenmann H. and Ransom B. R., eds), Oxford University Press, New York
    • Hamprecht B. and Dringen R. (1995) Energy metabolism, in Neuroglia (Kettenmann H. and Ransom B. R., eds), pp. 473-487. Oxford University Press, New York.
    • (1995) Neuroglia , pp. 473-487
    • Hamprecht, B.1    Dringen, R.2
  • 27
    • 0021893839 scopus 로고
    • Primary glial cultures as a model system for studying hormone action
    • Hamprecht B. and Löffler F. (1985) Primary glial cultures as a model system for studying hormone action. Methods Enzymol. 109, 341-345.
    • (1985) Methods Enzymol. , vol.109 , pp. 341-345
    • Hamprecht, B.1    Löffler, F.2
  • 28
    • 0024374913 scopus 로고
    • The role of selenium-dependent and selenium-independent glutathione peroxidase in the formation of prostaglandin F2 alpha
    • Hong Y., Li C. H., Burgess J. R., Chang M., Salem A., Srikumar K., and Reddy C. C. (1989) The role of selenium-dependent and selenium-independent glutathione peroxidase in the formation of prostaglandin F2 alpha. J. Biol. Chem. 264, 13793-13800.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13793-13800
    • Hong, Y.1    Li, C.H.2    Burgess, J.R.3    Chang, M.4    Salem, A.5    Srikumar, K.6    Reddy, C.C.7
  • 29
    • 0343374214 scopus 로고
    • Glucose metabolism in brain tissue: The hexosemonophosphate shunt and its role in glutathione reduction
    • Hotta S. S. (1962) Glucose metabolism in brain tissue: the hexosemonophosphate shunt and its role in glutathione reduction. J. Neurochem. 9, 43-51.
    • (1962) J. Neurochem. , vol.9 , pp. 43-51
    • Hotta, S.S.1
  • 30
    • 0014238709 scopus 로고
    • The hexosemonophosphate shunt and glutathione reduction in guinea pig brain tissue: Changes caused by chlorpromazine, amytal, and malonate
    • Hotta S. S. and Seventko J. M. Jr. (1968) The hexosemonophosphate shunt and glutathione reduction in guinea pig brain tissue: changes caused by chlorpromazine, amytal, and malonate. Arch. Biochem. Biophys. 123, 104-108.
    • (1968) Arch. Biochem. Biophys. , vol.123 , pp. 104-108
    • Hotta, S.S.1    Seventko J.M., Jr.2
  • 31
    • 0029050628 scopus 로고
    • Distribution of glutathione and glutathione-related enzyme systems in mitochondria and cytosol of cultured cerebellar astrocytes and granule cells
    • Huang J. and Philbert M. A. (1995) Distribution of glutathione and glutathione-related enzyme systems in mitochondria and cytosol of cultured cerebellar astrocytes and granule cells. Brain Res. 680, 16-22.
    • (1995) Brain Res. , vol.680 , pp. 16-22
    • Huang, J.1    Philbert, M.A.2
  • 33
    • 0025534063 scopus 로고
    • Oxygen radical generation in human platelets: Dependence on 12-lipoxygenase activity and on the glutathione cycle
    • Jahn B. and Hansch G. M. (1990) Oxygen radical generation in human platelets: dependence on 12-lipoxygenase activity and on the glutathione cycle. Int. Arch. Allergy Appl. Immunol. 93, 73-79.
    • (1990) Int. Arch. Allergy Appl. Immunol. , vol.93 , pp. 73-79
    • Jahn, B.1    Hansch, G.M.2
  • 35
    • 0025293777 scopus 로고
    • Hydrogen peroxide production during experimental protein glycation
    • Jiang Z.-Y., Woollard A. C. S., and Wolff S. P. (1990) Hydrogen peroxide production during experimental protein glycation. FEBS Lett. 268, 69-71.
    • (1990) FEBS Lett. , vol.268 , pp. 69-71
    • Jiang, Z.-Y.1    Woollard, A.C.S.2    Wolff, S.P.3
  • 36
    • 0022649760 scopus 로고
    • Immunocytochemical characterization of neuron-rich primary cultures of embryonic rat brain cells by established neuronal and glial markers and by monospecific antisera against cyclic nucleotide-dependent protein kinases and the synaptic vesicle protein synapsin I
    • Löffler F., Lohmann S. M., Walckhoff B., Walter U., and Hamprecht B. (1986) Immunocytochemical characterization of neuron-rich primary cultures of embryonic rat brain cells by established neuronal and glial markers and by monospecific antisera against cyclic nucleotide-dependent protein kinases and the synaptic vesicle protein synapsin I. Brain Res. 363, 205-221.
    • (1986) Brain Res. , vol.363 , pp. 205-221
    • Löffler, F.1    Lohmann, S.M.2    Walckhoff, B.3    Walter, U.4    Hamprecht, B.5
  • 38
    • 0027972577 scopus 로고
    • Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts
    • Makino N., Mochizuki Y., Bannai S., and Sugita Y. (1994) Kinetic studies on the removal of extracellular hydrogen peroxide by cultured fibroblasts. J. Biol. Chem. 269, 1020-1025.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1020-1025
    • Makino, N.1    Mochizuki, Y.2    Bannai, S.3    Sugita, Y.4
  • 39
    • 0028922502 scopus 로고
    • Kinetic studies on the removal of extracellular tert-butyl hydroperoxide by cultured fibroblasts
    • Makino N., Bannai S., and Sugita Y. (1995) Kinetic studies on the removal of extracellular tert-butyl hydroperoxide by cultured fibroblasts. Biochim. Biophys. Acta 1243, 503-508.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 503-508
    • Makino, N.1    Bannai, S.2    Sugita, Y.3
  • 40
    • 0026555334 scopus 로고
    • Depletion of brain glutathione by buthionine sulfoximine enhances cerebral ischemic injury in rats
    • Mizui T., Kinouchi H., and Chan P. H. (1992) Depletion of brain glutathione by buthionine sulfoximine enhances cerebral ischemic injury in rats. Am. J. Physiol. 262, H313-H317.
    • (1992) Am. J. Physiol. , vol.262
    • Mizui, T.1    Kinouchi, H.2    Chan, P.H.3
  • 41
    • 0024256996 scopus 로고
    • Astrocytes as eicosanoid-producing cells
    • Murphy S., Pearce B., Jeremy J., and Dandona P. (1988) Astrocytes as eicosanoid-producing cells. Glia 1, 241-245.
    • (1988) Glia , vol.1 , pp. 241-245
    • Murphy, S.1    Pearce, B.2    Jeremy, J.3    Dandona, P.4
  • 42
    • 0024537271 scopus 로고
    • Reduction of brain glutathione by L-buthionine sulfoximine potentiates the dopamine-depleting action of 6-hydroxydopamine in rat striatum
    • Pileblad E., Magnusson T., and Fornstedt B. (1989) Reduction of brain glutathione by L-buthionine sulfoximine potentiates the dopamine-depleting action of 6-hydroxydopamine in rat striatum. J. Neurochem. 52, 978-980.
    • (1989) J. Neurochem. , vol.52 , pp. 978-980
    • Pileblad, E.1    Magnusson, T.2    Fornstedt, B.3
  • 43
    • 0028010036 scopus 로고
    • Eicosanoids in synaptic transmission
    • Piomelli D. (1994) Eicosanoids in synaptic transmission. Crit. Rev. Neurobiol. 8, 65-83.
    • (1994) Crit. Rev. Neurobiol. , vol.8 , pp. 65-83
    • Piomelli, D.1
  • 44
    • 0024324666 scopus 로고
    • Glutathione is present in high concentrations in cultured astrocytes but not in cultured neurons
    • Raps S. P., Lai J. C. K., Hertz L., and Cooper A. J. L. (1989) Glutathione is present in high concentrations in cultured astrocytes but not in cultured neurons. Brain Res. 493, 3:98-401.
    • (1989) Brain Res. , vol.493 , pp. 398-401
    • Raps, S.P.1    Lai, J.C.K.2    Hertz, L.3    Cooper, A.J.L.4
  • 45
    • 0025247999 scopus 로고
    • Purification of glycogen phosphorylase from bovine brain and immunocytochemical examination of rat glial primary cultures using monoclonal antibodies raised against this enzyme
    • Reinhart P. H., Pfeiffer B., Spengler S., and Hamprecht B. (1990) Purification of glycogen phosphorylase from bovine brain and immunocytochemical examination of rat glial primary cultures using monoclonal antibodies raised against this enzyme. J. Neurochem. 54, 1474-1483.
    • (1990) J. Neurochem. , vol.54 , pp. 1474-1483
    • Reinhart, P.H.1    Pfeiffer, B.2    Spengler, S.3    Hamprecht, B.4
  • 46
    • 0016426055 scopus 로고
    • A simple cytochemical technique for demonstration of DNA in cells infected with mycoplasmas and viruses
    • Russel W. C., Newman G., and Williamson D. H. (1975) A simple cytochemical technique for demonstration of DNA in cells infected with mycoplasmas and viruses. Nature 253, 461-462.
    • (1975) Nature , vol.253 , pp. 461-462
    • Russel, W.C.1    Newman, G.2    Williamson, D.H.3
  • 47
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J., Dexter D. T., Lees A. J., Daniel S., Path M. R. C., Agid Y., Javoy-Agid F., Jenner P., and Marsden C. D. (1994) Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann. Neurol. 36, 348-355.
    • (1994) Ann. Neurol. , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Path, M.R.C.5    Agid, Y.6    Javoy-Agid, F.7    Jenner, P.8    Marsden, C.D.9
  • 48
    • 0018853019 scopus 로고
    • Hydrogen peroxide production by rat brain in vivo
    • Sinet P. M., Heikkila R. E., and Cohen G. (1980) Hydrogen peroxide production by rat brain in vivo. J. Neurochem. 34, 1421-1428.
    • (1980) J. Neurochem. , vol.34 , pp. 1421-1428
    • Sinet, P.M.1    Heikkila, R.E.2    Cohen, G.3
  • 49
    • 0026644192 scopus 로고
    • Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease
    • Sofic E., Lange K. W., Jellinger K., and Riederer P. (1992) Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci. Lett. 142, 128-130.
    • (1992) Neurosci. Lett. , vol.142 , pp. 128-130
    • Sofic, E.1    Lange, K.W.2    Jellinger, K.3    Riederer, P.4
  • 50
    • 0016218384 scopus 로고
    • Useful agents for the study of glutathione metabolism in erythrocytes
    • Srivastava S. K., Awasthi Y. C., and Beutler E. (1974) Useful agents for the study of glutathione metabolism in erythrocytes. Biochem. J. 139, 289-295.
    • (1974) Biochem. J. , vol.139 , pp. 289-295
    • Srivastava, S.K.1    Awasthi, Y.C.2    Beutler, E.3
  • 51
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze F. (1969) Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27, 502-522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 52
    • 0000191753 scopus 로고
    • Lactate dehydrogenase: UV-method with pyruvate and NADH
    • (Bergmeyer H. U., ed), Verlag Chemie, Weinheim, Germany
    • Vassault A. (1983) Lactate dehydrogenase: UV-method with pyruvate and NADH, in Methods of Enzymatic Analysis, Vol. 3 (Bergmeyer H. U., ed), pp. 118-126. Verlag Chemie, Weinheim, Germany.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 118-126
    • Vassault, A.1
  • 53
    • 0031782834 scopus 로고    scopus 로고
    • Mitochondrial malic enzyme: Purification from bovine brain, generation of an antiserum, and immunocytochemical localization in neurons of rat brain
    • Vogel R., Jennemann G., Seitz J., Wiesinger H., and Hamprecht B. (1998) Mitochondrial malic enzyme: purification from bovine brain, generation of an antiserum, and immunocytochemical localization in neurons of rat brain. J. Neurochem. 71, 844-852.
    • (1998) J. Neurochem. , vol.71 , pp. 844-852
    • Vogel, R.1    Jennemann, G.2    Seitz, J.3    Wiesinger, H.4    Hamprecht, B.5
  • 54
    • 0028072369 scopus 로고
    • The pathophysiology of reactive oxygen intermediates in the central nervous system
    • Weber G. F. (1994) The pathophysiology of reactive oxygen intermediates in the central nervous system. Med. Hypotheses 43, 223-230.
    • (1994) Med. Hypotheses , vol.43 , pp. 223-230
    • Weber, G.F.1


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