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Volumn 44, Issue 6, 2010, Pages 541-551

Establishment of steady-state metabolism of ethanol in perfused rat liver: The quantitative analysis using kinetic mechanism-based rate equations of alcohol dehydrogenase

Author keywords

Acetaldehyde; Acetate; Alcohol dehydrogenase; Aldehyde dehydroenase; Rat liver perfusion; Steady state metabolism of ethanol

Indexed keywords

4 METHYLPYRAZOLE; ACETALDEHYDE; ACETIC ACID; ALCOHOL; ALCOHOL DEHYDROGENASE; ENZYME INHIBITOR; ISOBUTYRAMIDE; LACTIC ACID; PYRUVIC ACID; UNCLASSIFIED DRUG;

EID: 77956629392     PISSN: 07418329     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.alcohol.2010.07.002     Document Type: Article
Times cited : (14)

References (57)
  • 1
    • 0015520615 scopus 로고
    • State of oxidation-reduction and state of binding in the cytosolic NADH-system as disclosed by equilibration with extracellular lactate-pyruvate in hemoglobin-free perfused rat liver
    • Bücher T., Brauser B., Conze A., Klein F., Langguth O., Sies H. State of oxidation-reduction and state of binding in the cytosolic NADH-system as disclosed by equilibration with extracellular lactate-pyruvate in hemoglobin-free perfused rat liver. Eur. J. Biochem. 1972, 27:301-317.
    • (1972) Eur. J. Biochem. , vol.27 , pp. 301-317
    • Bücher, T.1    Brauser, B.2    Conze, A.3    Klein, F.4    Langguth, O.5    Sies, H.6
  • 2
    • 0010526730 scopus 로고    scopus 로고
    • Metabolism of ethanol, acetaldehyde, and condensation products
    • Oxford University Press, Oxford, H. Begleiter, B. Kissin (Eds.)
    • Cederbaum A.I. Metabolism of ethanol, acetaldehyde, and condensation products. The Pharmacology of Alcohol and Alcohol Dependence 1996, 59-109. Oxford University Press, Oxford. H. Begleiter, B. Kissin (Eds.).
    • (1996) The Pharmacology of Alcohol and Alcohol Dependence , pp. 59-109
    • Cederbaum, A.I.1
  • 3
    • 59049104586 scopus 로고    scopus 로고
    • Polymorphism of ethanol-metabolism genes and alcoholism: correlation of allelic variations with the pharmacokinetic and pharmacodynamic consequences
    • Chen Y.C., Peng G.S., Wang M.F., Tsao T.P., Yin S.J. Polymorphism of ethanol-metabolism genes and alcoholism: correlation of allelic variations with the pharmacokinetic and pharmacodynamic consequences. Chem. Biol. Interact. 2009, 178:2-7.
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 2-7
    • Chen, Y.C.1    Peng, G.S.2    Wang, M.F.3    Tsao, T.P.4    Yin, S.J.5
  • 4
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland W.W. Statistical analysis of enzyme kinetic data. Methods Enzymol. 1979, 63:103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 5
    • 0021140604 scopus 로고
    • Properties of alcohol dehydrogenase and ethanol oxidation in vivo and in hepatocytes
    • Cornell N.W. Properties of alcohol dehydrogenase and ethanol oxidation in vivo and in hepatocytes. Pharmacol. Biochem. Behav. 1983, (18 Suppl 1):215-221.
    • (1983) Pharmacol. Biochem. Behav. , Issue.18 SUPPL. 1 , pp. 215-221
    • Cornell, N.W.1
  • 6
    • 0342732312 scopus 로고
    • Rate-limiting factors for ethanol oxidation in vivo and in isolated hepatocytes
    • U.S. Government Printing Office, Washington, DC, T.K. Li, S. Schenker, L. Lumeng (Eds.)
    • Cornell N.W., Crow K.E., Leadbetter M.G., Veech R.L. Rate-limiting factors for ethanol oxidation in vivo and in isolated hepatocytes. Alcohol and Nutrition 1979, 315-330. U.S. Government Printing Office, Washington, DC. T.K. Li, S. Schenker, L. Lumeng (Eds.).
    • (1979) Alcohol and Nutrition , pp. 315-330
    • Cornell, N.W.1    Crow, K.E.2    Leadbetter, M.G.3    Veech, R.L.4
  • 7
    • 0028844807 scopus 로고
    • Ethanol oxidizing enzymes: roles in alcohol metabolism and alcoholic liver disease
    • Crabb D.W. Ethanol oxidizing enzymes: roles in alcohol metabolism and alcoholic liver disease. Prog. Liver Dis. 1995, 13:151-172.
    • (1995) Prog. Liver Dis. , vol.13 , pp. 151-172
    • Crabb, D.W.1
  • 8
    • 0020791660 scopus 로고
    • Steady-state kinetic properties of purified rat liver alcohol dehydrogenase: application to predicting alcohol elimination rates in vivo
    • Crabb D.W., Bosron W.F., Li T.K. Steady-state kinetic properties of purified rat liver alcohol dehydrogenase: application to predicting alcohol elimination rates in vivo. Arch. Biochem. Biophys. 1983, 224:299-309.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 299-309
    • Crabb, D.W.1    Bosron, W.F.2    Li, T.K.3
  • 9
  • 10
    • 0019944747 scopus 로고
    • The D(V/K) isotope effect of the cytochrome P-450-mediated oxidation of ethanol and its biological applications
    • Damgaard S.E. The D(V/K) isotope effect of the cytochrome P-450-mediated oxidation of ethanol and its biological applications. Eur. J. Biochem. 1982, 125:593-603.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 593-603
    • Damgaard, S.E.1
  • 12
    • 0018859318 scopus 로고
    • Determination of hepatic acetaldehyde and its biphasic relationship to the ethanol concentration in rats
    • Eriksson C.J.P. Determination of hepatic acetaldehyde and its biphasic relationship to the ethanol concentration in rats. Adv. Exp. Med. Biol. 1980, 132:459-467.
    • (1980) Adv. Exp. Med. Biol. , vol.132 , pp. 459-467
    • Eriksson, C.J.P.1
  • 13
    • 0035815751 scopus 로고    scopus 로고
    • Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate
    • Fujino T., Kondo J., Ishikawa M., Morikawa K., Yamamoto T.T. Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in the oxidation of acetate. J. Biol. Chem. 2001, 276:11420-11426.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11420-11426
    • Fujino, T.1    Kondo, J.2    Ishikawa, M.3    Morikawa, K.4    Yamamoto, T.T.5
  • 14
    • 0022462510 scopus 로고
    • Semiautomated analysis of ethanol and acetate in human plasma by head space gas chromatography
    • Giles H.G., Meggiorini S., Vidins E.I. Semiautomated analysis of ethanol and acetate in human plasma by head space gas chromatography. Can. J. Physiol. Pharmacol. 1986, 64:717-719.
    • (1986) Can. J. Physiol. Pharmacol. , vol.64 , pp. 717-719
    • Giles, H.G.1    Meggiorini, S.2    Vidins, E.I.3
  • 15
    • 0015890975 scopus 로고
    • Rate-limiting factors in ethanol oxidation by isolated rat-liver parenchymal cells: effect of ethanol concentration, fructose, pyruvate and pyrazole
    • Grunnet N., Quistorff B., Thieden H.I. Rate-limiting factors in ethanol oxidation by isolated rat-liver parenchymal cells: effect of ethanol concentration, fructose, pyruvate and pyrazole. Eur. J. Biochem. 1973, 40:275-282.
    • (1973) Eur. J. Biochem. , vol.40 , pp. 275-282
    • Grunnet, N.1    Quistorff, B.2    Thieden, H.I.3
  • 17
    • 0015989446 scopus 로고
    • A linear steady-state treatment of enzymatic chains: critique of the crossover theorem and a general procedure to identify interaction sites with an effector
    • Heinrich R., Rapoport T.A. A linear steady-state treatment of enzymatic chains: critique of the crossover theorem and a general procedure to identify interaction sites with an effector. Eur. J. Biochem. 1974, 42:89-95.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 89-95
    • Heinrich, R.1    Rapoport, T.A.2
  • 18
    • 0011927177 scopus 로고
    • Control of ethanol oxidation and its interaction with other metabolic systems
    • Plenum Press, New York, E. Majchrowicz, E.P. Noble (Eds.)
    • Higgins J.J. Control of ethanol oxidation and its interaction with other metabolic systems. Biochemistry and Pharmacology of Ethanol 1979, 249-351. Plenum Press, New York. E. Majchrowicz, E.P. Noble (Eds.).
    • (1979) Biochemistry and Pharmacology of Ethanol , pp. 249-351
    • Higgins, J.J.1
  • 19
    • 0015824267 scopus 로고
    • The control of flux
    • Reprinted (with additional comments by H. Kacser and D.A. Fell) in Biochem. Soc. Trans. 23, 341-366, 1995
    • Kacser H., Burns J.A. The control of flux. Symp. Soc. Exp. Biol. 1973, 27:65-104. Reprinted (with additional comments by H. Kacser and D.A. Fell) in Biochem. Soc. Trans. 23, 341-366, 1995.
    • (1973) Symp. Soc. Exp. Biol. , vol.27 , pp. 65-104
    • Kacser, H.1    Burns, J.A.2
  • 20
    • 0021209947 scopus 로고
    • Current models of hepatic pharmacokinetics: flow effects on kinetic constants of ethanol elimination in perfused rat liver
    • Keiding S., Priisholm K. Current models of hepatic pharmacokinetics: flow effects on kinetic constants of ethanol elimination in perfused rat liver. Biochem. Pharmacol. 1984, 33:3209-3212.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 3209-3212
    • Keiding, S.1    Priisholm, K.2
  • 21
    • 0024986951 scopus 로고
    • Ethanol metabolism and alcoholic liver disease
    • Kennedy N.P., Tipton K.F. Ethanol metabolism and alcoholic liver disease. Essays Biochem. 1990, 25:137-195.
    • (1990) Essays Biochem. , vol.25 , pp. 137-195
    • Kennedy, N.P.1    Tipton, K.F.2
  • 23
    • 0029935028 scopus 로고    scopus 로고
    • Possible role of liver cytosolic and mitochondrial aldehyde dehydrogenases in acetaldehyde metabolism
    • Klyosov A.A., Rashkovetsky L.G., Tahir M.K., Keung W.M. Possible role of liver cytosolic and mitochondrial aldehyde dehydrogenases in acetaldehyde metabolism. Biochemistry 1996, 35:4445-4456.
    • (1996) Biochemistry , vol.35 , pp. 4445-4456
    • Klyosov, A.A.1    Rashkovetsky, L.G.2    Tahir, M.K.3    Keung, W.M.4
  • 25
    • 0001206338 scopus 로고
    • Pyruvate
    • Verlag Chemie, Weinheim, H.U. Bergmeyer (Ed.)
    • Lamprecht W., Heinz F. Pyruvate. Methods of Enzymatic Analysis 1984, Vol. 6:570-577. Verlag Chemie, Weinheim. 3rd ed. H.U. Bergmeyer (Ed.).
    • (1984) Methods of Enzymatic Analysis , vol.6 , pp. 570-577
    • Lamprecht, W.1    Heinz, F.2
  • 26
    • 0017079895 scopus 로고
    • Double-ternary complex affinity chromatography: preparation of alcohol dehydrogenases
    • Lange L.G., Vallee B.L. Double-ternary complex affinity chromatography: preparation of alcohol dehydrogenases. Biochemistry 1976, 15:4681-4686.
    • (1976) Biochemistry , vol.15 , pp. 4681-4686
    • Lange, L.G.1    Vallee, B.L.2
  • 27
    • 0022634648 scopus 로고
    • Presence of nonoxidative ethanol metabolism in human organs commonly damaged by ethanol abuse
    • Laposata E.A., Lange L.G. Presence of nonoxidative ethanol metabolism in human organs commonly damaged by ethanol abuse. Science 1986, 231:497-499.
    • (1986) Science , vol.231 , pp. 497-499
    • Laposata, E.A.1    Lange, L.G.2
  • 28
    • 33745146510 scopus 로고    scopus 로고
    • Functional assessment of human alcohol dehydrogenase family in ethanol metabolism: significance of first-pass metabolism
    • Lee S.L., Chau G.Y., Yao C.T., Wu C.W., Yin S.J. Functional assessment of human alcohol dehydrogenase family in ethanol metabolism: significance of first-pass metabolism. Alcohol. Clin. Exp. Res. 2006, 30:1132-1142.
    • (2006) Alcohol. Clin. Exp. Res. , vol.30 , pp. 1132-1142
    • Lee, S.L.1    Chau, G.Y.2    Yao, C.T.3    Wu, C.W.4    Yin, S.J.5
  • 29
    • 0015298144 scopus 로고
    • Utilization and metabolic effects of acetaldehyde and ethanol in the perfused rat liver
    • Lindros K.O., Vihma R., Forsander O.A. Utilization and metabolic effects of acetaldehyde and ethanol in the perfused rat liver. Biochem. J. 1972, 126:945-952.
    • (1972) Biochem. J. , vol.126 , pp. 945-952
    • Lindros, K.O.1    Vihma, R.2    Forsander, O.A.3
  • 31
    • 0018749938 scopus 로고
    • Quantitative correlation of ethanol elimination rates in vivo with liver alcohol dehydrogenase activities in fed, fasted and food-restricted rats
    • Lumeng L., Bosron W.F., Li T.K. Quantitative correlation of ethanol elimination rates in vivo with liver alcohol dehydrogenase activities in fed, fasted and food-restricted rats. Biochem. Pharmacol. 1979, 28:1547-1551.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 1547-1551
    • Lumeng, L.1    Bosron, W.F.2    Li, T.K.3
  • 32
    • 0024372765 scopus 로고
    • Deuterium isotope effects on ethanol oxidation in perfused rat liver and in rats and rabbits in vivo: application to determine the contribution of various pathways
    • Lundquist F., Quistorff B., Huang M.T. Deuterium isotope effects on ethanol oxidation in perfused rat liver and in rats and rabbits in vivo: application to determine the contribution of various pathways. Pharmacol. Toxicol. 1989, 65:55-62.
    • (1989) Pharmacol. Toxicol. , vol.65 , pp. 55-62
    • Lundquist, F.1    Quistorff, B.2    Huang, M.T.3
  • 33
    • 0022838986 scopus 로고
    • The deuterium isotope effect on ethanol metabolism in perfused rat liver: effect of reversed perfusion on ethanol and oxygen uptake
    • Lundquist F., Quistorff B., Iversen H. The deuterium isotope effect on ethanol metabolism in perfused rat liver: effect of reversed perfusion on ethanol and oxygen uptake. Alcohol. Clin. Exp. Res. 1986, 10:69S-72S.
    • (1986) Alcohol. Clin. Exp. Res. , vol.10
    • Lundquist, F.1    Quistorff, B.2    Iversen, H.3
  • 34
    • 0034714382 scopus 로고    scopus 로고
    • Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins
    • Luong A., Hannah V.C., Brown M.S., Goldstein J.L. Molecular characterization of human acetyl-CoA synthetase, an enzyme regulated by sterol regulatory element-binding proteins. J. Biol. Chem. 2000, 275:26458-26466.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26458-26466
    • Luong, A.1    Hannah, V.C.2    Brown, M.S.3    Goldstein, J.L.4
  • 35
    • 0001486532 scopus 로고
    • L-(+)-lactate
    • Verlag Chemie, Weinheim, H.U. Bergmeyer (Ed.)
    • Noll F. L-(+)-lactate. Methods of Enzymatic Analysis 1984, Vol. 6:582-588. Verlag Chemie, Weinheim. 3rd ed. H.U. Bergmeyer (Ed.).
    • (1984) Methods of Enzymatic Analysis , vol.6 , pp. 582-588
    • Noll, F.1
  • 36
    • 0021223675 scopus 로고
    • Blood acetaldehyde concentration gradient between hepatic and antecubital venous blood in ethanol-intoxicated alcoholics and controls
    • Nuutinen H.U., Salaspuro M.P., Valle M., Lindros K.O. Blood acetaldehyde concentration gradient between hepatic and antecubital venous blood in ethanol-intoxicated alcoholics and controls. Eur. J. Clin. Invest. 1984, 14:306-311.
    • (1984) Eur. J. Clin. Invest. , vol.14 , pp. 306-311
    • Nuutinen, H.U.1    Salaspuro, M.P.2    Valle, M.3    Lindros, K.O.4
  • 37
    • 0025826138 scopus 로고
    • The importance of alcohol dehydrogenase in regulation of ethanol metabolism in rat liver cells
    • Page R.A., Kitson K.E., Hardman M.J. The importance of alcohol dehydrogenase in regulation of ethanol metabolism in rat liver cells. Biochem. J. 1991, 278:659-665.
    • (1991) Biochem. J. , vol.278 , pp. 659-665
    • Page, R.A.1    Kitson, K.E.2    Hardman, M.J.3
  • 38
    • 74549208493 scopus 로고    scopus 로고
    • Alterations in brain glucose utilization accompanying elevations in blood ethanol and acetate concentrations in the rat
    • Pawlosky R.J., Kashiwaya Y., Srivastava S., King M.T., Crutchfield C., Volkow N., et al. Alterations in brain glucose utilization accompanying elevations in blood ethanol and acetate concentrations in the rat. Alcohol. Clin. Exp. Res. 2010, 34:375-381.
    • (2010) Alcohol. Clin. Exp. Res. , vol.34 , pp. 375-381
    • Pawlosky, R.J.1    Kashiwaya, Y.2    Srivastava, S.3    King, M.T.4    Crutchfield, C.5    Volkow, N.6
  • 39
    • 0032872033 scopus 로고    scopus 로고
    • Involvement of acetaldehyde for full protection against alcoholism by homozygosity of the variant allele of mitochondrial aldehyde dehydrogenase gene in Asians
    • Peng G.S., Wang M.F., Chen C.Y., Luu S.U., Chou H.C., Li T.K., et al. Involvement of acetaldehyde for full protection against alcoholism by homozygosity of the variant allele of mitochondrial aldehyde dehydrogenase gene in Asians. Pharmacogenetics 1999, 9:463-476.
    • (1999) Pharmacogenetics , vol.9 , pp. 463-476
    • Peng, G.S.1    Wang, M.F.2    Chen, C.Y.3    Luu, S.U.4    Chou, H.C.5    Li, T.K.6
  • 40
    • 0021251601 scopus 로고
    • Kinetics of inhibition of ethanol metabolism in rats and the rate-limiting role of alcohol dehydrogenase
    • Plapp B.V., Leidal K.G., Smith R.K., Murch B.P. Kinetics of inhibition of ethanol metabolism in rats and the rate-limiting role of alcohol dehydrogenase. Arch. Biochem. Biophys. 1984, 230:30-38.
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 30-38
    • Plapp, B.V.1    Leidal, K.G.2    Smith, R.K.3    Murch, B.P.4
  • 41
    • 0035969862 scopus 로고    scopus 로고
    • Mouse alcohol dehydrogenase 4: kinetic mechanism, substrate specificity and simulation of effects of ethanol on retinoid metabolism
    • Plapp B.V., Mitchell J.L., Berst K.B. Mouse alcohol dehydrogenase 4: kinetic mechanism, substrate specificity and simulation of effects of ethanol on retinoid metabolism. Chem. Biol. Interact. 2001, 130-132:445-456.
    • (2001) Chem. Biol. Interact. , pp. 445-456
    • Plapp, B.V.1    Mitchell, J.L.2    Berst, K.B.3
  • 42
    • 34547622816 scopus 로고    scopus 로고
    • Sex differences, alcohol dehydrogenase, acetaldehyde burst, and aversion to ethanol in the rat: a systems perspective
    • Quintanilla M.E., Tampier L., Sapag A., Gerdtzen Z., Israel Y. Sex differences, alcohol dehydrogenase, acetaldehyde burst, and aversion to ethanol in the rat: a systems perspective. Am. J. Physiol. Endocrinol. Metab. 2007, 293:E531-E537.
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.293
    • Quintanilla, M.E.1    Tampier, L.2    Sapag, A.3    Gerdtzen, Z.4    Israel, Y.5
  • 43
    • 0019418553 scopus 로고
    • Liver blood flow. I. Intrinsic and nervous control of liver blood flow
    • Richardson P.D., Withrington P.G. Liver blood flow. I. Intrinsic and nervous control of liver blood flow. Gastroenterology 1981, 81:159-173.
    • (1981) Gastroenterology , vol.81 , pp. 159-173
    • Richardson, P.D.1    Withrington, P.G.2
  • 44
    • 75149178671 scopus 로고    scopus 로고
    • Mechanism of protection against alcoholism by an alcohol dehydrogenase polymorphism: development of an animal model
    • Rivera-Meza M., Quintanilla M.E., Tampier L., Mura C.V., Sapag A., Israel Y. Mechanism of protection against alcoholism by an alcohol dehydrogenase polymorphism: development of an animal model. FASEB J. 2010, 24:266-274.
    • (2010) FASEB J. , vol.24 , pp. 266-274
    • Rivera-Meza, M.1    Quintanilla, M.E.2    Tampier, L.3    Mura, C.V.4    Sapag, A.5    Israel, Y.6
  • 45
    • 0347154530 scopus 로고
    • Lactate dehydrogenase
    • Academic Press, New York, P.D. Boyer, H. Lardy, K. Myrback (Eds.)
    • Schwert G.W., Winer A.D. Lactate dehydrogenase. The Enzymes 1963, Vol. 7:127-148. Academic Press, New York. P.D. Boyer, H. Lardy, K. Myrback (Eds.).
    • (1963) The Enzymes , vol.7 , pp. 127-148
    • Schwert, G.W.1    Winer, A.D.2
  • 46
    • 0032716189 scopus 로고    scopus 로고
    • De novo lipogenesis, lipid kinetics, and whole-body lipid balances in humans after acute alcohol consumption
    • Siler S.Q., Neese R.A., Hellerstein M.K. De novo lipogenesis, lipid kinetics, and whole-body lipid balances in humans after acute alcohol consumption. Am. J. Clin. Nutr. 1999, 70:928-936.
    • (1999) Am. J. Clin. Nutr. , vol.70 , pp. 928-936
    • Siler, S.Q.1    Neese, R.A.2    Hellerstein, M.K.3
  • 48
    • 0022357937 scopus 로고
    • The effect of acute ethanol treatment on rates of oxygen uptake, ethanol oxidation and gluconeogenesis in isolated rat hepatocytes
    • Stowell K.M., Crow K.E. The effect of acute ethanol treatment on rates of oxygen uptake, ethanol oxidation and gluconeogenesis in isolated rat hepatocytes. Biochem. J. 1985, 230:595-602.
    • (1985) Biochem. J. , vol.230 , pp. 595-602
    • Stowell, K.M.1    Crow, K.E.2
  • 49
    • 0015278655 scopus 로고
    • Control of the redox state of the nicotinamide-adenine dinucleotide couple in rat liver cytoplasm
    • Stubbs M., Veech R.L., Krebs H.A. Control of the redox state of the nicotinamide-adenine dinucleotide couple in rat liver cytoplasm. Biochem. J. 1972, 126:59-65.
    • (1972) Biochem. J. , vol.126 , pp. 59-65
    • Stubbs, M.1    Veech, R.L.2    Krebs, H.A.3
  • 50
    • 0003077255 scopus 로고
    • Alcohol dehydrogenases
    • Academic Press, New York, P.D. Boyer, H. Lardy, K. Myrback (Eds.)
    • Sund H., Theorell H. Alcohol dehydrogenases. The Enzymes 1963, Vol. 7:25-83. Academic Press, New York. P.D. Boyer, H. Lardy, K. Myrback (Eds.).
    • (1963) The Enzymes , vol.7 , pp. 25-83
    • Sund, H.1    Theorell, H.2
  • 51
    • 0344132637 scopus 로고    scopus 로고
    • A novel subtype of class II alcohol dehydrogenase in rodents: unique Pro(47) and Ser(182) modulates hydride transfer in the mouse enzyme
    • Svensson S., Stromberg P., Hoog J.O. A novel subtype of class II alcohol dehydrogenase in rodents: unique Pro(47) and Ser(182) modulates hydride transfer in the mouse enzyme. J. Biol. Chem. 1999, 274:29712-29719.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29712-29719
    • Svensson, S.1    Stromberg, P.2    Hoog, J.O.3
  • 52
    • 0015326154 scopus 로고
    • The time-course of the effects of ethanol on the redox and phosphorylation states of rat liver
    • Veech R.L., Guynn R., Veloso D. The time-course of the effects of ethanol on the redox and phosphorylation states of rat liver. Biochem. J. 1972, 127:387-397.
    • (1972) Biochem. J. , vol.127 , pp. 387-397
    • Veech, R.L.1    Guynn, R.2    Veloso, D.3
  • 53
    • 59049089641 scopus 로고    scopus 로고
    • Substrate specificity of human and yeast aldehyde dehydrogenases
    • Wang M.F., Han C.L., Yin S.J. Substrate specificity of human and yeast aldehyde dehydrogenases. Chem. Biol. Interact. 2009, 178:36-39.
    • (2009) Chem. Biol. Interact. , vol.178 , pp. 36-39
    • Wang, M.F.1    Han, C.L.2    Yin, S.J.3
  • 54
    • 0021360023 scopus 로고
    • Modern theories of metabolic control and their applications
    • Westerhoff H.V., Groen A.K., Wanders R.J. Modern theories of metabolic control and their applications. Biosci. Rep. 1984, 4:1-22.
    • (1984) Biosci. Rep. , vol.4 , pp. 1-22
    • Westerhoff, H.V.1    Groen, A.K.2    Wanders, R.J.3
  • 55
    • 0035978425 scopus 로고    scopus 로고
    • Production of acetate in the liver and its utilization in peripheral tissues
    • Yamashita H., Kaneyuki T., Tagawa K. Production of acetate in the liver and its utilization in peripheral tissues. Biochim. Biophys. Acta 2001, 1532:79-87.
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 79-87
    • Yamashita, H.1    Kaneyuki, T.2    Tagawa, K.3
  • 56
    • 0011920383 scopus 로고
    • On the ternary complex of liver alcohol dehydrogenase with reduced coenzyme and isobutyramide: effect of p-chloromercuriphenyl sulfonate and stability of the complex
    • Yonetani T., Theorell H. On the ternary complex of liver alcohol dehydrogenase with reduced coenzyme and isobutyramide: effect of p-chloromercuriphenyl sulfonate and stability of the complex. Arch. Biochem. Biophys. 1962, 99:433-446.
    • (1962) Arch. Biochem. Biophys. , vol.99 , pp. 433-446
    • Yonetani, T.1    Theorell, H.2
  • 57
    • 37749053679 scopus 로고    scopus 로고
    • Determinants of alcohol use and abuse: impact of quantity and frequency patterns on liver disease
    • Zakhari S., Li T.K. Determinants of alcohol use and abuse: impact of quantity and frequency patterns on liver disease. Hepatology 2007, 46:2032-2039.
    • (2007) Hepatology , vol.46 , pp. 2032-2039
    • Zakhari, S.1    Li, T.K.2


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