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Volumn 124, Issue 3, 1999, Pages 225-230

Mitochondrial aldehyde dehydrogenase from the liver of skipjack tuna Katsuwonus pelamis

Author keywords

Aldehyde dehydrogenase; Liver; Mitochondria; Properties; Purification; Skipjack tuna

Indexed keywords

ACETALDEHYDE; ALDEHYDE DEHYDROGENASE; ALDEHYDE DERIVATIVE; BENZALDEHYDE; ISOENZYME; LIVER ENZYME; MITOCHONDRIAL ENZYME; PROPIONALDEHYDE; SEROTONIN;

EID: 0032692554     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(99)00041-3     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0015237332 scopus 로고
    • Genetic aspects of increase in rat liver aldehyde dehydrogenase induced by phenobarbital
    • Deitrich RA. Genetic aspects of increase in rat liver aldehyde dehydrogenase induced by phenobarbital. Science 1971;173:334-6.
    • (1971) Science , vol.173 , pp. 334-336
    • Deitrich, R.A.1
  • 2
    • 0015523893 scopus 로고
    • Genetic influence upon phenobarbital-induced increase in rat liver aldehyde dehydrogenase activity
    • Deitrich RA, Collins AC, Erwin VG. Genetic influence upon phenobarbital-induced increase in rat liver aldehyde dehydrogenase activity. J Biol Chem 1972;247:7232-6.
    • (1972) J Biol Chem , vol.247 , pp. 7232-7236
    • Deitrich, R.A.1    Collins, A.C.2    Erwin, V.G.3
  • 4
    • 0017253860 scopus 로고
    • Horse liver aldehyde dehydrogenase: Purification and characterization of two isozymes
    • Eckfeldt J, Mope L, Takio K, Yonetani T. Horse liver aldehyde dehydrogenase: purification and characterization of two isozymes. J Biol Chem 1976;251:236-40.
    • (1976) J Biol Chem , vol.251 , pp. 236-240
    • Eckfeldt, J.1    Mope, L.2    Takio, K.3    Yonetani, T.4
  • 5
    • 0015499904 scopus 로고
    • Horse liver aldehyde dehydrogenase. Purification and characterization
    • Feldman RI, Weiner H. Horse liver aldehyde dehydrogenase. Purification and characterization. J Biol Chem 1972;247:260-6.
    • (1972) J Biol Chem , vol.247 , pp. 260-266
    • Feldman, R.I.1    Weiner, H.2
  • 6
    • 0017406798 scopus 로고
    • Two aldehyde dehydrogenase from human liver. Isolation via affinity chromatography and characterization of the isoenzyme
    • Greenfield NJ, Pietruszko R. Two aldehyde dehydrogenase from human liver. Isolation via affinity chromatography and characterization of the isoenzyme. Biochim Biophys Acta 1977;483:35-45.
    • (1977) Biochim Biophys Acta , vol.483 , pp. 35-45
    • Greenfield, N.J.1    Pietruszko, R.2
  • 7
    • 0020553805 scopus 로고
    • Utilization of the ethanol pathway in carp following exposure to anoxia
    • Johnston IA, Bernhard LM. Utilization of the ethanol pathway in carp following exposure to anoxia. J Exp Biol 1983;104:73-8.
    • (1983) J Exp Biol , vol.104 , pp. 73-78
    • Johnston, I.A.1    Bernhard, L.M.2
  • 8
    • 0014430406 scopus 로고
    • Isolation and characterization of human aldehyde dehydrogenase
    • Kraemer RJ, Deitrich RA. Isolation and characterization of human aldehyde dehydrogenase. J Biol Chem 1968;243:6402-8.
    • (1968) J Biol Chem , vol.243 , pp. 6402-6408
    • Kraemer, R.J.1    Deitrich, R.A.2
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assem-bly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assem-bly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 13044268853 scopus 로고
    • Rat liver aldehyde dehydrogenase. Isolation and characterization of four inducible isozymes
    • Lindall R, Evces S. Rat liver aldehyde dehydrogenase. Isolation and characterization of four inducible isozymes. J Biol Chem 1984;259:265-75.
    • (1984) J Biol Chem , vol.259 , pp. 265-275
    • Lindall, R.1    Evces, S.2
  • 15
    • 0020480047 scopus 로고
    • Anaerobic metabolism of red skeletal muscle of goldfish, Carassius auratus (L.)
    • Mourik J, Raeven P, Steur K, Addink ADF. Anaerobic metabolism of red skeletal muscle of goldfish, Carassius auratus (L.). FEBS Lett 1982;137:111-4.
    • (1982) FEBS Lett , vol.137 , pp. 111-114
    • Mourik, J.1    Raeven, P.2    Steur, K.3    Addink, A.D.F.4
  • 16
    • 85010174864 scopus 로고
    • Purification and properties of skipjack liver tryptophan hydroxylase
    • Nagai T, Serrano AE Jr., Nagayama F. Purification and properties of skipjack liver tryptophan hydroxylase. Fisheries Sci 1994;60:445-8.
    • (1994) Fisheries Sci , vol.60 , pp. 445-448
    • Nagai, T.1    Serrano Jr., A.E.2    Nagayama, F.3
  • 17
    • 0028804029 scopus 로고
    • Purification and properties of aromatic L-amino acid decarboxylase from liver of skipjack tuna (Katsuwonus pelamis, Teleostei: Scombridae)
    • Nagai T, Hamada M, Kai N, Tanoue Y, Nagayama F. Purification and properties of aromatic L-amino acid decarboxylase from liver of skipjack tuna (Katsuwonus pelamis, Teleostei: Scombridae). Comp Biochem Physiol 1995;112B:265-70.
    • (1995) Comp Biochem Physiol , vol.112 B , pp. 265-270
    • Nagai, T.1    Hamada, M.2    Kai, N.3    Tanoue, Y.4    Nagayama, F.5
  • 18
    • 85008131314 scopus 로고
    • Organ distribution of aldehyde dehydrogenase activity of several fish
    • Nagai T, Hamada M, Kai N, Tanoue Y, Nagayama F. Organ distribution of aldehyde dehydrogenase activity of several fish. Fisheries Sci 1995;61:1047-8.
    • (1995) Fisheries Sci , vol.61 , pp. 1047-1048
    • Nagai, T.1    Hamada, M.2    Kai, N.3    Tanoue, Y.4    Nagayama, F.5
  • 19
    • 0346391946 scopus 로고    scopus 로고
    • Purification and characterization of alcohol dehydrogenase from liver of skipjack Katsuwonus pelamis
    • Nagai T, Hamada M, Kai N, Tanoue Y, Nagayama F. Purification and characterization of alcohol dehydrogenase from liver of skipjack Katsuwonus pelamis. Fisheries Sci 1996;62:272-7.
    • (1996) Fisheries Sci , vol.62 , pp. 272-277
    • Nagai, T.1    Hamada, M.2    Kai, N.3    Tanoue, Y.4    Nagayama, F.5
  • 20
    • 0030940953 scopus 로고    scopus 로고
    • A novel type mitochondrial monoamine oxidase from the liver of skipjack tuna (Katsuwonus pelamis): Purification and characterisation
    • Nagai T, Hamada M, Kai N, Tanoue Y, Nagayama F. A novel type mitochondrial monoamine oxidase from the liver of skipjack tuna (Katsuwonus pelamis): purification and characterisation. J Sci Food Agric 1997;73:489-93.
    • (1997) J Sci Food Agric , vol.73 , pp. 489-493
    • Nagai, T.1    Hamada, M.2    Kai, N.3    Tanoue, Y.4    Nagayama, F.5
  • 21
    • 0030889376 scopus 로고    scopus 로고
    • Characterization of yellowfin tuna (Thunnus albacares, Scombroidei) tryptophan hydroxylase
    • Nagai T, Hamada M, Kai N, Tanoue Y, Nagayama F. Characterization of yellowfin tuna (Thunnus albacares, Scombroidei) tryptophan hydroxylase. Comp Biochem Physiol 1997;116B: 161-5.
    • (1997) Comp Biochem Physiol , vol.116 B , pp. 161-165
    • Nagai, T.1    Hamada, M.2    Kai, N.3    Tanoue, Y.4    Nagayama, F.5
  • 22
    • 0022372321 scopus 로고
    • Biogenic aldehyde in brain: Characteristics of a reaction between rat brain tissue and indole-3-acetaldehyde
    • Nilsson GE, Tottmar O. Biogenic aldehyde in brain: characteristics of a reaction between rat brain tissue and indole-3-acetaldehyde. J Neurochem 1985;45:744-51.
    • (1985) J Neurochem , vol.45 , pp. 744-751
    • Nilsson, G.E.1    Tottmar, O.2
  • 23
    • 0023191825 scopus 로고
    • Biogenic aldehyde in brain: On their preparation and reactions with rat brain tissue
    • Nilsson GE, Tottmar O. Biogenic aldehyde in brain: on their preparation and reactions with rat brain tissue. J Neurochem 1987;48:1566-72.
    • (1987) J Neurochem , vol.48 , pp. 1566-1572
    • Nilsson, G.E.1    Tottmar, O.2
  • 24
    • 0024225880 scopus 로고
    • A comparative study on aldehyde dehydrogenase and alcohol dehydrogenase activities in crucian carp and three other vertebrates: Apparent adaptations to ethanol production
    • Nilsson GE. A comparative study on aldehyde dehydrogenase and alcohol dehydrogenase activities in crucian carp and three other vertebrates: apparent adaptations to ethanol production. J Comp Physiol B 1988;158:479-85.
    • (1988) J Comp Physiol B , vol.158 , pp. 479-485
    • Nilsson, G.E.1
  • 25
    • 0023744780 scopus 로고
    • Organ distribution of aldehyde dehydrogenase activity in the rainbow trout (Salmo gairdneri richardson)
    • Nilsson GE. Organ distribution of aldehyde dehydrogenase activity in the rainbow trout (Salmo gairdneri richardson). Comp Biochem Physiol 1988;90B:109-11.
    • (1988) Comp Biochem Physiol , vol.90 B , pp. 109-111
    • Nilsson, G.E.1
  • 26
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson GL. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal Biochem 1977;83:346-56.
    • (1977) Anal Biochem , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 27
    • 13044295227 scopus 로고
    • Acetaldehyde oxidation in molybdenum deficiency
    • Richert DA, Westerfeld WW. Acetaldehyde oxidation in molybdenum deficiency. J Biol Chem 1957;227:533-6.
    • (1957) J Biol Chem , vol.227 , pp. 533-536
    • Richert, D.A.1    Westerfeld, W.W.2
  • 28
    • 0023353186 scopus 로고
    • Purification and characterization of aldehyde dehydrogenase from human brain
    • Ryzlak MT, Pietruszko R. Purification and characterization of aldehyde dehydrogenase from human brain. Arch Biochem Biophys 1987;255:409-18.
    • (1987) Arch Biochem Biophys , vol.255 , pp. 409-418
    • Ryzlak, M.T.1    Pietruszko, R.2
  • 29
    • 0021848489 scopus 로고
    • Canine liver aldehyde dehydrogenases: Distribution, isolation, and partial characterization
    • Sanny CG. Canine liver aldehyde dehydrogenases: distribution, isolation, and partial characterization. Alcohol Clin Exp Res 1985;9:255-62.
    • (1985) Alcohol Clin Exp Res , vol.9 , pp. 255-262
    • Sanny, C.G.1
  • 30
    • 0019312446 scopus 로고
    • Ethanol: Novel end product of vertebrate anaerobic metabolism
    • Shoubridge EA, Hochachka PW. Ethanol: novel end product of vertebrate anaerobic metabolism. Science 1980;209:308-9.
    • (1980) Science , vol.209 , pp. 308-309
    • Shoubridge, E.A.1    Hochachka, P.W.2
  • 31
    • 0019820895 scopus 로고
    • The origin and significance of metabolic carbon dioxide production in the anoxic goldfish
    • Shoubridge EA, Hochachka PW. The origin and significance of metabolic carbon dioxide production in the anoxic goldfish. Molec Physiol 1981;1:315-38.
    • (1981) Molec Physiol , vol.1 , pp. 315-338
    • Shoubridge, E.A.1    Hochachka, P.W.2
  • 32
    • 0014429124 scopus 로고
    • Yeast aldehyde dehydrogenase. Properties of the homogeneous enzyme preparations
    • Steinman CR, Jakoby WB. Yeast aldehyde dehydrogenase. Properties of the homogeneous enzyme preparations. J Biol Chem 1968;243:730-4.
    • (1968) J Biol Chem , vol.243 , pp. 730-734
    • Steinman, C.R.1    Jakoby, W.B.2
  • 33
    • 0343705980 scopus 로고
    • Enzymic improvement of food flavor. Purification and characterization of bovine liver mitochondrial aldehyde dehydrogenase
    • Takahashi N, Kitabatake N, Sasaki R, Chiba H. Enzymic improvement of food flavor. Purification and characterization of bovine liver mitochondrial aldehyde dehydrogenase. Agric Biol Chem 1979;43:1873-82.
    • (1979) Agric Biol Chem , vol.43 , pp. 1873-1882
    • Takahashi, N.1    Kitabatake, N.2    Sasaki, R.3    Chiba, H.4
  • 34
    • 0014429643 scopus 로고
    • Aldehyde dehydrogenase. Purification and properties of the enzyme from Pseudomonas aeruginosa
    • Tigerstrom RGV, Razzel WE. Aldehyde dehydrogenase. Purification and properties of the enzyme from Pseudomonas aeruginosa. J Biol Chem 1968;243:2691-702.
    • (1968) J Biol Chem , vol.243 , pp. 2691-2702
    • Tigerstrom, R.G.V.1    Razzel, W.E.2


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