메뉴 건너뛰기




Volumn 48, Issue 6-7, 2006, Pages 629-636

Aspartate aminotransferase in synaptic and nonsynaptic mitochondria: Differential effect of compounds that influence transient hetero-enzyme complex (metabolon) formation

Author keywords

Ketoglutarate; Aspartate aminotransferase; Bovine serum albumin; Citrate; Complexes; Enzyme regulation; Glutamate; Malate; Metabolism; Mg2+; Mitochondrial binding; Nonsynaptic mitochondria; Palmitate; Synaptic mitochondria; Transient hetero enzyme

Indexed keywords

ASPARTATE AMINOTRANSFERASE; BOVINE SERUM ALBUMIN; CITRIC ACID; GLUTAMIC ACID; MAGNESIUM ION; MALIC ACID; MULTIENZYME COMPLEX; PALMITIC ACID;

EID: 33645894184     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuint.2005.11.018     Document Type: Article
Times cited : (37)

References (60)
  • 1
    • 0019588210 scopus 로고
    • Demonstration of physical interactions between consecutive enzymes of the citric acid cycle and the aspartate-malate shuttle. A study involving fumarase, malate dehydrogenase, citrate synthesis and aspartate aminotransferase
    • Beeckmans S., and Kanarek L. Demonstration of physical interactions between consecutive enzymes of the citric acid cycle and the aspartate-malate shuttle. A study involving fumarase, malate dehydrogenase, citrate synthesis and aspartate aminotransferase. Eur. J. Biochem. 117 (1981) 527-535
    • (1981) Eur. J. Biochem. , vol.117 , pp. 527-535
    • Beeckmans, S.1    Kanarek, L.2
  • 2
    • 0025146192 scopus 로고
    • Clustering of sequential enzymes in the glycolytic pathway and the citric acid cycle
    • Beeckmans S., Van Driessche E., and Kanarek L. Clustering of sequential enzymes in the glycolytic pathway and the citric acid cycle. J. Cell. Biochem. 43 (1990) 297-306
    • (1990) J. Cell. Biochem. , vol.43 , pp. 297-306
    • Beeckmans, S.1    Van Driessche, E.2    Kanarek, L.3
  • 3
    • 0001062128 scopus 로고
    • Aspartate aminotransferase
    • Academic Press, New York pp. 416-424
    • Bergmeyer H.U. Aspartate aminotransferase. Methods in Enzymatic Analysis (1974), Academic Press, New York pp. 416-424
    • (1974) Methods in Enzymatic Analysis
    • Bergmeyer, H.U.1
  • 5
    • 0034141834 scopus 로고    scopus 로고
    • Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA
    • Bradbury M.W., and Berk P.D. Mitochondrial aspartate aminotransferase: direction of a single protein with two distinct functions to two subcellular sites does not require alternative splicing of the mRNA. Biochem. J. 345 Pt 3 (2000) 423-427
    • (2000) Biochem. J. , vol.345 , Issue.PART 3 , pp. 423-427
    • Bradbury, M.W.1    Berk, P.D.2
  • 6
    • 2342572890 scopus 로고    scopus 로고
    • Regulation of glutamate-synthesizing enzymes by NMDA and potassium in cerebellar granule cells
    • Caballero-Benitez A., Alavez S., Uribe R.M., and Moran J. Regulation of glutamate-synthesizing enzymes by NMDA and potassium in cerebellar granule cells. Eur. J. Neurosci. 19 (2004) 2030-2038
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 2030-2038
    • Caballero-Benitez, A.1    Alavez, S.2    Uribe, R.M.3    Moran, J.4
  • 7
    • 0028966538 scopus 로고
    • Immunocytochemical examination of neural rat and mouse primary cultures using monoclonal antibodies raised against pyruvate carboxylase
    • Cesar M., and Hamprecht B. Immunocytochemical examination of neural rat and mouse primary cultures using monoclonal antibodies raised against pyruvate carboxylase. J. Neurochem. 64 (1995) 2312-2318
    • (1995) J. Neurochem. , vol.64 , pp. 2312-2318
    • Cesar, M.1    Hamprecht, B.2
  • 8
    • 0023879595 scopus 로고
    • Influence of the malate-aspartate shuttle on oxidative metabolism in synaptosomes
    • Cheeseman A.J., and Clark J.B. Influence of the malate-aspartate shuttle on oxidative metabolism in synaptosomes. J. Neurochem. 50 (1988) 1559-1565
    • (1988) J. Neurochem. , vol.50 , pp. 1559-1565
    • Cheeseman, A.J.1    Clark, J.B.2
  • 9
    • 0001792169 scopus 로고
    • Metabolic significance of transamination
    • Wiley, New York pp. 500-580
    • Cooper A.J., and Meister A. Metabolic significance of transamination. Transaminases (1985), Wiley, New York pp. 500-580
    • (1985) Transaminases
    • Cooper, A.J.1    Meister, A.2
  • 10
    • 0021111842 scopus 로고
    • Binding of citrate synthase to mitochondrial inner membranes
    • D'Souza S.F., and Srere P.A. Binding of citrate synthase to mitochondrial inner membranes. J. Biol. Chem. 258 (1983) 4706-4709
    • (1983) J. Biol. Chem. , vol.258 , pp. 4706-4709
    • D'Souza, S.F.1    Srere, P.A.2
  • 11
    • 0017350802 scopus 로고
    • Effect of aspartate on complexes between glutamate dehydrogenase and various aminotransferases
    • Fahien L.A., Hsu S.L., and Kmiotek E. Effect of aspartate on complexes between glutamate dehydrogenase and various aminotransferases. J. Biol. Chem. 252 (1977) 1250-1256
    • (1977) J. Biol. Chem. , vol.252 , pp. 1250-1256
    • Fahien, L.A.1    Hsu, S.L.2    Kmiotek, E.3
  • 12
    • 0020713005 scopus 로고
    • Complexes between mitochondrial enzymes and either citrate synthase or glutamate dehydrogenase
    • Fahien L.A., and Kmiotek E. Complexes between mitochondrial enzymes and either citrate synthase or glutamate dehydrogenase. Arch. Biochem. Biophys. 220 (1983) 386-397
    • (1983) Arch. Biochem. Biophys. , vol.220 , pp. 386-397
    • Fahien, L.A.1    Kmiotek, E.2
  • 13
    • 0023761140 scopus 로고
    • Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction
    • Fahien L.A., Kmiotek E.H., MacDonald M.J., Fibich B., and Mandic M. Regulation of malate dehydrogenase activity by glutamate, citrate, alpha-ketoglutarate, and multienzyme interaction. J. Biol. Chem. 263 (1988) 10687-10697
    • (1988) J. Biol. Chem. , vol.263 , pp. 10687-10697
    • Fahien, L.A.1    Kmiotek, E.H.2    MacDonald, M.J.3    Fibich, B.4    Mandic, M.5
  • 14
    • 0021276164 scopus 로고
    • Interactions between carbamyl phosphate synthase-I-mitochondrial aspartate aminotransferase and palmitoyl-CoA
    • Fahien L.A., Kmiotek E.H., and Marshall M. Interactions between carbamyl phosphate synthase-I-mitochondrial aspartate aminotransferase and palmitoyl-CoA. Arch. Biochem. Biophys. 230 (1984) 213-221
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 213-221
    • Fahien, L.A.1    Kmiotek, E.H.2    Marshall, M.3
  • 16
    • 0024361268 scopus 로고
    • Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the alpha-ketoglutarate dehydrogenase complex
    • Fahien L.A., MacDonald M.J., Teller J.K., Fibich B., and Fahien C.M. Kinetic advantages of hetero-enzyme complexes with glutamate dehydrogenase and the alpha-ketoglutarate dehydrogenase complex. J. Biol. Chem. 264 (1989) 12303-12312
    • (1989) J. Biol. Chem. , vol.264 , pp. 12303-12312
    • Fahien, L.A.1    MacDonald, M.J.2    Teller, J.K.3    Fibich, B.4    Fahien, C.M.5
  • 17
    • 0026698788 scopus 로고
    • Glutamate-malate metabolism in liver mitochondria. A model constructed on the basis of mitochondrial levels of enzymes, specificity, dissociation constants, and stoichiometry of hetero-enzyme complexes
    • Fahien L.A., and Teller J.K. Glutamate-malate metabolism in liver mitochondria. A model constructed on the basis of mitochondrial levels of enzymes, specificity, dissociation constants, and stoichiometry of hetero-enzyme complexes. J. Biol. Chem. 267 (1992) 10411-10422
    • (1992) J. Biol. Chem. , vol.267 , pp. 10411-10422
    • Fahien, L.A.1    Teller, J.K.2
  • 19
    • 0021062309 scopus 로고
    • Use of beta-methylene-d,l-aspartate to assess the role of aspartate aminotransferase in cerebral oxidative metabolism
    • Fitzpatrick S.M., Cooper A.J., and Duffy T.E. Use of beta-methylene-d,l-aspartate to assess the role of aspartate aminotransferase in cerebral oxidative metabolism. J. Neurochem. 41 (1983) 1370-1383
    • (1983) J. Neurochem. , vol.41 , pp. 1370-1383
    • Fitzpatrick, S.M.1    Cooper, A.J.2    Duffy, T.E.3
  • 20
    • 0037646540 scopus 로고    scopus 로고
    • Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis
    • Hayashi H., Mizuguchi H., Miyahara I., Nakajima Y., Hirotsu K., and Kagamiyama H. Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis. J. Biol. Chem. 278 (2003) 9481-9488
    • (2003) J. Biol. Chem. , vol.278 , pp. 9481-9488
    • Hayashi, H.1    Mizuguchi, H.2    Miyahara, I.3    Nakajima, Y.4    Hirotsu, K.5    Kagamiyama, H.6
  • 21
    • 85052763520 scopus 로고
    • Metabolism of glutamate and glutamine in neurons and astrocytes in primary cultures
    • Kvamme E. (Ed), CRC Press, Boca Raton pp. 39-56
    • Hertz L., and Schousboe A. Metabolism of glutamate and glutamine in neurons and astrocytes in primary cultures. In: Kvamme E. (Ed). Glutamate and Glutamine in Mammals (1988), CRC Press, Boca Raton pp. 39-56
    • (1988) Glutamate and Glutamine in Mammals
    • Hertz, L.1    Schousboe, A.2
  • 22
    • 0028786938 scopus 로고
    • 3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake
    • Isola L.M., Zhou S.L., Kiang C.L., Stump D.D., Bradbury M.W., and Berk P.D. 3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 9866-9870
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9866-9870
    • Isola, L.M.1    Zhou, S.L.2    Kiang, C.L.3    Stump, D.D.4    Bradbury, M.W.5    Berk, P.D.6
  • 23
    • 0034098693 scopus 로고    scopus 로고
    • The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase
    • Jeffery C.J., Gloss L.M., Petsko G.A., and Ringe D. The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase. Protein Eng. 13 (2000) 105-112
    • (2000) Protein Eng. , vol.13 , pp. 105-112
    • Jeffery, C.J.1    Gloss, L.M.2    Petsko, G.A.3    Ringe, D.4
  • 24
    • 0018338308 scopus 로고
    • Preparation of synaptic and nonsynaptic mitochondria from the mammalian brain
    • Academic Press, New York pp. 51-59
    • Lai J.C., and Clark J.B. Preparation of synaptic and nonsynaptic mitochondria from the mammalian brain. Methods in Enzymology (1979), Academic Press, New York pp. 51-59
    • (1979) Methods in Enzymology
    • Lai, J.C.1    Clark, J.B.2
  • 25
    • 0003046064 scopus 로고
    • Isolation and characterization of synaptic and nonsynaptic mitochondria from the mammalian brain
    • Humana Press, Clifton, NJ pp. 43-98
    • Lai J.C., and Clark J.B. Isolation and characterization of synaptic and nonsynaptic mitochondria from the mammalian brain. Neuromethods, Carbohydrates and Energy Metabolism (1989), Humana Press, Clifton, NJ pp. 43-98
    • (1989) Neuromethods, Carbohydrates and Energy Metabolism
    • Lai, J.C.1    Clark, J.B.2
  • 26
    • 0017344533 scopus 로고
    • Synaptic and non-synaptic mitochondria from rat brain: isolation and characterization
    • Lai J.C., Walsh J.M., Dennis S.C., and Clark J.B. Synaptic and non-synaptic mitochondria from rat brain: isolation and characterization. J. Neurochem. 28 (1977) 625-631
    • (1977) J. Neurochem. , vol.28 , pp. 625-631
    • Lai, J.C.1    Walsh, J.M.2    Dennis, S.C.3    Clark, J.B.4
  • 27
    • 0027412177 scopus 로고
    • Regulation of malate dehydrogenases from neonatal, adolescent, and mature rat brain
    • Malik P., McKenna M.C., and Tildon J.T. Regulation of malate dehydrogenases from neonatal, adolescent, and mature rat brain. Neurochem. Res. 18 (1993) 247-257
    • (1993) Neurochem. Res. , vol.18 , pp. 247-257
    • Malik, P.1    McKenna, M.C.2    Tildon, J.T.3
  • 28
    • 0034256931 scopus 로고    scopus 로고
    • Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals
    • McKenna M.C., Stevenson J.H., Huang X., and Hopkins I.B. Differential distribution of the enzymes glutamate dehydrogenase and aspartate aminotransferase in cortical synaptic mitochondria contributes to metabolic compartmentation in cortical synaptic terminals. Neurochem. Int. 37 (2000) 229-241
    • (2000) Neurochem. Int. , vol.37 , pp. 229-241
    • McKenna, M.C.1    Stevenson, J.H.2    Huang, X.3    Hopkins, I.B.4
  • 29
    • 0033982623 scopus 로고    scopus 로고
    • Mitochondrial malic enzyme activity is much higher in mitochondria from cortical synaptic terminals compared with mitochondria from primary cultures of cortical neurons or cerebellar granule cells
    • McKenna M.C., Stevenson J.H., Huang X., Tildon J.T., Zielke C.L., and Hopkins I.B. Mitochondrial malic enzyme activity is much higher in mitochondria from cortical synaptic terminals compared with mitochondria from primary cultures of cortical neurons or cerebellar granule cells. Neurochem. Int. 36 (2000) 451-459
    • (2000) Neurochem. Int. , vol.36 , pp. 451-459
    • McKenna, M.C.1    Stevenson, J.H.2    Huang, X.3    Tildon, J.T.4    Zielke, C.L.5    Hopkins, I.B.6
  • 31
    • 0027727915 scopus 로고
    • Regulation of energy metabolism in synaptic terminals and cultured rat brain astrocytes: differences revealed using aminooxyacetate
    • McKenna M.C., Tildon J.T., Stevenson J.H., Boatright R., and Huang S. Regulation of energy metabolism in synaptic terminals and cultured rat brain astrocytes: differences revealed using aminooxyacetate. Dev. Neurosci. 15 (1993) 320-329
    • (1993) Dev. Neurosci. , vol.15 , pp. 320-329
    • McKenna, M.C.1    Tildon, J.T.2    Stevenson, J.H.3    Boatright, R.4    Huang, S.5
  • 32
    • 0028658335 scopus 로고
    • Energy metabolism in cortical synaptic terminals from weanling and mature rat brain: evidence for multiple compartments of tricarboxylic acid cycle activity
    • McKenna M.C., Tildon J.T., Stevenson J.H., and Hopkins I.B. Energy metabolism in cortical synaptic terminals from weanling and mature rat brain: evidence for multiple compartments of tricarboxylic acid cycle activity. Dev. Neurosci. 16 (1994) 291-300
    • (1994) Dev. Neurosci. , vol.16 , pp. 291-300
    • McKenna, M.C.1    Tildon, J.T.2    Stevenson, J.H.3    Hopkins, I.B.4
  • 33
    • 0029972176 scopus 로고    scopus 로고
    • New insights into the compartmentation of glutamate and glutamine in cultured rat brain astrocytes
    • McKenna M.C., Tildon J.T., Stevenson J.H., and Huang X. New insights into the compartmentation of glutamate and glutamine in cultured rat brain astrocytes. Dev. Neurosci. 18 (1996) 380-390
    • (1996) Dev. Neurosci. , vol.18 , pp. 380-390
    • McKenna, M.C.1    Tildon, J.T.2    Stevenson, J.H.3    Huang, X.4
  • 34
    • 0029619279 scopus 로고
    • Regulation of mitochondrial and cytosolic malic enzymes from cultured rat brain astrocytes
    • McKenna M.C., Tildon J.T., Stevenson J.H., Huang X., and Kingwell K.G. Regulation of mitochondrial and cytosolic malic enzymes from cultured rat brain astrocytes. Neurochem. Res. 20 (1995) 1491-1501
    • (1995) Neurochem. Res. , vol.20 , pp. 1491-1501
    • McKenna, M.C.1    Tildon, J.T.2    Stevenson, J.H.3    Huang, X.4    Kingwell, K.G.5
  • 35
    • 30444437034 scopus 로고    scopus 로고
    • Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: current evidence and pharmacological tools
    • McKenna M.C., Waagepetersen H.S., Schousboe A., and Sonnewald U. Neuronal and astrocytic shuttle mechanisms for cytosolic-mitochondrial transfer of reducing equivalents: current evidence and pharmacological tools. Biochem. Pharmacol. 71 (2006) 399-407
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 399-407
    • McKenna, M.C.1    Waagepetersen, H.S.2    Schousboe, A.3    Sonnewald, U.4
  • 36
    • 0032978023 scopus 로고    scopus 로고
    • Effect of NMDA antagonists on the activity of glutaminase and aspartate aminotransferase in the developing rat cerebellum
    • Moran J., Alavez S., Rivera-Gaxiola M., Valencia A., and Hurtado S. Effect of NMDA antagonists on the activity of glutaminase and aspartate aminotransferase in the developing rat cerebellum. Int. J. Dev. Neurosci. 17 (1999) 57-65
    • (1999) Int. J. Dev. Neurosci. , vol.17 , pp. 57-65
    • Moran, J.1    Alavez, S.2    Rivera-Gaxiola, M.3    Valencia, A.4    Hurtado, S.5
  • 37
    • 0026698927 scopus 로고
    • Effect of potassium and N-methyl-d-aspartate on the aspartate aminotransferase activity in cultured cerebellar granule cells
    • Moran J., and Rivera-Gaxiola M. Effect of potassium and N-methyl-d-aspartate on the aspartate aminotransferase activity in cultured cerebellar granule cells. J. Neurosci. Res. 33 (1992) 239-247
    • (1992) J. Neurosci. Res. , vol.33 , pp. 239-247
    • Moran, J.1    Rivera-Gaxiola, M.2
  • 38
    • 0023913351 scopus 로고
    • Evidence that aspartate aminotransferase activity and ketodicarboxylate carrier function are essential for biosynthesis of transmitter glutamate
    • Palaiologos G., Hertz L., and Schousboe A. Evidence that aspartate aminotransferase activity and ketodicarboxylate carrier function are essential for biosynthesis of transmitter glutamate. J. Neurochem. 51 (1988) 317-320
    • (1988) J. Neurochem. , vol.51 , pp. 317-320
    • Palaiologos, G.1    Hertz, L.2    Schousboe, A.3
  • 39
    • 0024411518 scopus 로고
    • Role of aspartate aminotransferase and mitochondrial dicarboxylate transport for release of endogenously and exogenously supplied neurotransmitter in glutamatergic neurons
    • Palaiologos G., Hertz L., and Schousboe A. Role of aspartate aminotransferase and mitochondrial dicarboxylate transport for release of endogenously and exogenously supplied neurotransmitter in glutamatergic neurons. Neurochem. Res. 14 (1989) 359-366
    • (1989) Neurochem. Res. , vol.14 , pp. 359-366
    • Palaiologos, G.1    Hertz, L.2    Schousboe, A.3
  • 40
    • 0020322196 scopus 로고
    • Abnormal glutamate metabolism in an adult-onset degenerative neurological disorder
    • Plaitakis A., Berl S., and Yahr M.D. Abnormal glutamate metabolism in an adult-onset degenerative neurological disorder. Science 216 (1982) 193-196
    • (1982) Science , vol.216 , pp. 193-196
    • Plaitakis, A.1    Berl, S.2    Yahr, M.D.3
  • 41
    • 0021340557 scopus 로고
    • Neurological disorders associated with deficiency of glutamate dehydrogenase
    • Plaitakis A., Berl S., and Yahr M.D. Neurological disorders associated with deficiency of glutamate dehydrogenase. Ann. Neurol. 15 (1984) 144-153
    • (1984) Ann. Neurol. , vol.15 , pp. 144-153
    • Plaitakis, A.1    Berl, S.2    Yahr, M.D.3
  • 43
    • 0027722238 scopus 로고
    • A developmental study of lactate dehydrogenase isozyme and aspartate aminotransferase activity in organotypic rat hippocampal slice cultures and primary cultures of mouse neocortical and cerebellar neurons
    • Schousboe I., Tonder N., Zimmer J., and Schousboe A. A developmental study of lactate dehydrogenase isozyme and aspartate aminotransferase activity in organotypic rat hippocampal slice cultures and primary cultures of mouse neocortical and cerebellar neurons. Int. J. Dev. Neurosci. 11 (1993) 765-772
    • (1993) Int. J. Dev. Neurosci. , vol.11 , pp. 765-772
    • Schousboe, I.1    Tonder, N.2    Zimmer, J.3    Schousboe, A.4
  • 44
    • 0027481105 scopus 로고
    • 2-Oxoglutarate transport: a potential mechanism for regulating glutamate and tricarboxylic acid cycle intermediates in neurons
    • Shank R.P., and Bennett D.J. 2-Oxoglutarate transport: a potential mechanism for regulating glutamate and tricarboxylic acid cycle intermediates in neurons. Neurochem. Res. 18 (1993) 401-410
    • (1993) Neurochem. Res. , vol.18 , pp. 401-410
    • Shank, R.P.1    Bennett, D.J.2
  • 47
    • 0031940131 scopus 로고    scopus 로고
    • Mitochondrial heterogeneity in the brain at the cellular level
    • Sonnewald U., Hertz L., and Schousboe A. Mitochondrial heterogeneity in the brain at the cellular level. J. Cereb. Blood Flow Metab. 18 (1998) 231-237
    • (1998) J. Cereb. Blood Flow Metab. , vol.18 , pp. 231-237
    • Sonnewald, U.1    Hertz, L.2    Schousboe, A.3
  • 50
    • 0031239422 scopus 로고    scopus 로고
    • Glutamate transport and metabolism in astrocytes
    • Sonnewald U., Westergaard N., and Schousboe A. Glutamate transport and metabolism in astrocytes. Glia 21 (1997) 56-63
    • (1997) Glia , vol.21 , pp. 56-63
    • Sonnewald, U.1    Westergaard, N.2    Schousboe, A.3
  • 51
    • 0027143338 scopus 로고
    • Comparison of plasma membrane FABP and mitochondrial isoform of aspartate aminotransferase from rat liver
    • Stump D.D., Zhou S.L., and Berk P.D. Comparison of plasma membrane FABP and mitochondrial isoform of aspartate aminotransferase from rat liver. Am. J. Physiol. 265 (1993) G894-G902
    • (1993) Am. J. Physiol. , vol.265
    • Stump, D.D.1    Zhou, S.L.2    Berk, P.D.3
  • 52
    • 0026660577 scopus 로고
    • Kinetics and regulation of hepatoma mitochondrial NAD(P) malic enzyme
    • Teller J.K., Fahien L.A., and Davis J.W. Kinetics and regulation of hepatoma mitochondrial NAD(P) malic enzyme. J. Biol. Chem. 267 (1992) 10423-10432
    • (1992) J. Biol. Chem. , vol.267 , pp. 10423-10432
    • Teller, J.K.1    Fahien, L.A.2    Davis, J.W.3
  • 53
    • 0025241173 scopus 로고
    • Interactions among mitochondrial aspartate aminotransferase, malate dehydrogenase, and the inner mitochondrial membrane from heart, hepatoma, and liver
    • Teller J.K., Fahien L.A., and Valdivia E. Interactions among mitochondrial aspartate aminotransferase, malate dehydrogenase, and the inner mitochondrial membrane from heart, hepatoma, and liver. J. Biol. Chem. 265 (1990) 19486-19494
    • (1990) J. Biol. Chem. , vol.265 , pp. 19486-19494
    • Teller, J.K.1    Fahien, L.A.2    Valdivia, E.3
  • 54
    • 0034846461 scopus 로고    scopus 로고
    • Multiple compartments with different metabolic characteristics are involved in biosynthesis of intracellular and released glutamine and citrate in astrocytes
    • Waagepetersen H.S., Sonnewald U., Larsson O.M., and Schousboe A. Multiple compartments with different metabolic characteristics are involved in biosynthesis of intracellular and released glutamine and citrate in astrocytes. Glia 35 (2001) 246-252
    • (2001) Glia , vol.35 , pp. 246-252
    • Waagepetersen, H.S.1    Sonnewald, U.2    Larsson, O.M.3    Schousboe, A.4
  • 58
    • 0035577702 scopus 로고    scopus 로고
    • Ketogenic diet, amino acid metabolism, and seizure control
    • Yudkoff M., Daikhin Y., Nissim I., and Lazarow A. Ketogenic diet, amino acid metabolism, and seizure control. J. Neurosci. Res. 66 (2001) 931-940
    • (2001) J. Neurosci. Res. , vol.66 , pp. 931-940
    • Yudkoff, M.1    Daikhin, Y.2    Nissim, I.3    Lazarow, A.4
  • 59
    • 0342750824 scopus 로고
    • Kinetics III-reversible inhibition of enzyme action
    • Wiley, New York pp. 87-99
    • Zeffren E., and Hall P.L. Kinetics III-reversible inhibition of enzyme action. The Study of Enzyme Mechanisms (1973), Wiley, New York pp. 87-99
    • (1973) The Study of Enzyme Mechanisms
    • Zeffren, E.1    Hall, P.L.2
  • 60
    • 0028905711 scopus 로고
    • Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake
    • Zhou S.L., Stump D., Kiang C.L., Isola L.M., and Berk P.D. Mitochondrial aspartate aminotransferase expressed on the surface of 3T3-L1 adipocytes mediates saturable fatty acid uptake. Proc. Soc. Exp. Biol. Med. 208 (1995) 263-270
    • (1995) Proc. Soc. Exp. Biol. Med. , vol.208 , pp. 263-270
    • Zhou, S.L.1    Stump, D.2    Kiang, C.L.3    Isola, L.M.4    Berk, P.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.