메뉴 건너뛰기




Volumn 28, Issue 8, 1996, Pages 873-881

Cytosolic aspartate aminotransferase from the grey mullet (Mugil auratus risso) red muscle: Isolation and properties

Author keywords

Aminotransferase; Aspartate; Cytosol; Enzyme characterization; Enzyme purification; Grey mullet

Indexed keywords

ASPARTATE AMINOTRANSFERASE; ISOENZYME;

EID: 0030220789     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/1357-2725(96)00033-7     Document Type: Article
Times cited : (10)

References (46)
  • 1
    • 0029066733 scopus 로고
    • Evaluation and modification of an assay procedure for cysteine dioxygenase activity: High-performance liquid chromatography method for measurement of cysteine sulfinate and demonstration of physiological relevance of cysteine dioxygenase activity in cysteine catabolism
    • Bagley P. J., Hirschberger L. L. and Stipanuk M. H. (1995) Evaluation and modification of an assay procedure for cysteine dioxygenase activity: high-performance liquid chromatography method for measurement of cysteine sulfinate and demonstration of physiological relevance of cysteine dioxygenase activity in cysteine catabolism. Analyt. Biochem. 227, 40-48.
    • (1995) Analyt. Biochem. , vol.227 , pp. 40-48
    • Bagley, P.J.1    Hirschberger, L.L.2    Stipanuk, M.H.3
  • 2
    • 0014428799 scopus 로고
    • The molecular weight and other properties of aspartate aminotransferase from pig heart muscle
    • Banks B. E. C., Doonan S., Lawrence A. J. and Vernon C. A. (1968) The molecular weight and other properties of aspartate aminotransferase from pig heart muscle. Eur. J. Biochem. 5, 528-539.
    • (1968) Eur. J. Biochem. , vol.5 , pp. 528-539
    • Banks, B.E.C.1    Doonan, S.2    Lawrence, A.J.3    Vernon, C.A.4
  • 3
    • 0014223604 scopus 로고
    • Chicken heart soluble aspartate aminotransferase: Purification and properties
    • Bertland L. H. and Kaplan N. O. (1968) Chicken heart soluble aspartate aminotransferase: Purification and properties. Biochemistry 7, 134-142.
    • (1968) Biochemistry , vol.7 , pp. 134-142
    • Bertland, L.H.1    Kaplan, N.O.2
  • 4
    • 0014959674 scopus 로고
    • Studies on the conformations of the multiple forms of chicken heart aspartate aminotransferase
    • Bertland L. H. and Kaplan N. O. (1970) Studies on the conformations of the multiple forms of chicken heart aspartate aminotransferase. Biochemistry 9, 2653-2665.
    • (1970) Biochemistry , vol.9 , pp. 2653-2665
    • Bertland, L.H.1    Kaplan, N.O.2
  • 5
    • 0000362380 scopus 로고
    • Biochemical aspects of fish swimming
    • Edited by Malins D. C. and Sargent J. R. Academic Press, New York
    • Bilinski E. (1974) Biochemical aspects of fish swimming. In Biochemical and Biophysical Perspectives in Marine Biology (Edited by Malins D. C. and Sargent J. R.), Vol. 1, pp. 239-288. Academic Press, New York.
    • (1974) Biochemical and Biophysical Perspectives in Marine Biology , vol.1 , pp. 239-288
    • Bilinski, E.1
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt. Biochem. 72, 248-254.
    • (1976) Analyt. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 77956923492 scopus 로고
    • Amino group transfer
    • Edited by Boyer P. D. Academic Press, New York
    • Braunstein A. E. (1973) Amino group transfer. In The Enzymes (Edited by Boyer P. D.), Vol. 9, pp. 379-481. Academic Press, New York.
    • (1973) The Enzymes , vol.9 , pp. 379-481
    • Braunstein, A.E.1
  • 8
    • 0015761090 scopus 로고
    • Purification and some properties of cytoplasmic aspatrate aminotransferase from sheep liver
    • Campos-Cavieres M. and Munn E. A. (1973) Purification and some properties of cytoplasmic aspatrate aminotransferase from sheep liver. Biochem. J. 135, 683-693.
    • (1973) Biochem. J. , vol.135 , pp. 683-693
    • Campos-Cavieres, M.1    Munn, E.A.2
  • 9
    • 0020641981 scopus 로고
    • Relationship of serum chemistry values to the liver and kidney histopathology in English sole (Parophrys vetulus) after acute exposure to carbon tetrachloride
    • Casillas E., Myers M. and Ames W. E. (1983) Relationship of serum chemistry values to the liver and kidney histopathology in English sole (Parophrys vetulus) after acute exposure to carbon tetrachloride. Aquat. Toxicol. 3, 61-78.
    • (1983) Aquat. Toxicol. , vol.3 , pp. 61-78
    • Casillas, E.1    Myers, M.2    Ames, W.E.3
  • 10
    • 0022530028 scopus 로고
    • 4 on English sole (Parophrys vetulus): Possible indicators of liver dysfunction
    • 4 on English sole (Parophrys vetulus): possible indicators of liver dysfunction. Comp. Biochem. Physiol. 84C, 397-400.
    • (1986) Comp. Biochem. Physiol. , vol.84 C , pp. 397-400
    • Casillas, E.1    Ames, W.E.2
  • 11
    • 0018142979 scopus 로고
    • Comparative aspects of adenylic acid deaminase and aspartate-2-oxoglutarate aminotransferase
    • Chandrasena S. I. and Hird F. J. R. (1978) Comparative aspects of adenylic acid deaminase and aspartate-2-oxoglutarate aminotransferase. Comp. Biochem. Physiol. 61B, 191-194.
    • (1978) Comp. Biochem. Physiol. , vol.61 B , pp. 191-194
    • Chandrasena, S.I.1    Hird, F.J.R.2
  • 12
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
    • Cleland W. W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. biophys. Acta 67, 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 13
    • 0018125902 scopus 로고
    • Comparative aspects of aminotransferases in the rat, pigeon and rainbow trout
    • Cornish E. C., Cussen C. M., Hird F. J. R. and Todd P. E. E. (1978) Comparative aspects of aminotransferases in the rat, pigeon and rainbow trout. Comp. Biochem. Physiol. 61B, 375-378.
    • (1978) Comp. Biochem. Physiol. , vol.61 B , pp. 375-378
    • Cornish, E.C.1    Cussen, C.M.2    Hird, F.J.R.3    Todd, P.E.E.4
  • 14
    • 0011805613 scopus 로고
    • Interspecies comparisons of aspartate aminotransferases based on amino acid compositions
    • Doonan S., Barra D., Bossa F., Porter P. B. and Wilkinson S. M. (1981) Interspecies comparisons of aspartate aminotransferases based on amino acid compositions. Comp. Biochem. Physiol. 69B, 747-752.
    • (1981) Comp. Biochem. Physiol. , vol.69 B , pp. 747-752
    • Doonan, S.1    Barra, D.2    Bossa, F.3    Porter, P.B.4    Wilkinson, S.M.5
  • 15
    • 0027212256 scopus 로고
    • Catabolism of cysteine, cystine, cysteinesulfinate, and OTC by isolated perfused rat hindquarter
    • Ensunsa J. L., Hirschberger L. L. and Stipanuk M. H. (1993) Catabolism of cysteine, cystine, cysteinesulfinate, and OTC by isolated perfused rat hindquarter. Am. J. Physiol. 264, E782-E789.
    • (1993) Am. J. Physiol. , vol.264
    • Ensunsa, J.L.1    Hirschberger, L.L.2    Stipanuk, M.H.3
  • 16
    • 84988112567 scopus 로고
    • Long term stability of colors after silver staining
    • Hempelmann E. and Kaminsky R. (1986) Long term stability of colors after silver staining. Electrophoresis 7, 481.
    • (1986) Electrophoresis , vol.7 , pp. 481
    • Hempelmann, E.1    Kaminsky, R.2
  • 17
    • 77049204706 scopus 로고
    • A note on the spectrophotometric assay of glutamic-oxalacetic transaminase in human blood serum
    • Karmen A. (1955) A note on the spectrophotometric assay of glutamic-oxalacetic transaminase in human blood serum. J. clin. Invest. 34, 131-133.
    • (1955) J. Clin. Invest. , vol.34 , pp. 131-133
    • Karmen, A.1
  • 18
    • 0000693866 scopus 로고
    • Estimation of the enzymes LDH, GOT and GPT in plasma of grey mullet Mugil auratus and their significance in liver intoxication
    • Krajnović-Ozretić M. and Ozretić B. (1987) Estimation of the enzymes LDH, GOT and GPT in plasma of grey mullet Mugil auratus and their significance in liver intoxication. Dis. aquat. Org. 3, 187-193.
    • (1987) Dis. Aquat. Org. , vol.3 , pp. 187-193
    • Krajnović-Ozretić, M.1    Ozretić, B.2
  • 19
    • 0015914931 scopus 로고
    • Beef brain cytoplasmic aspartate aminotransferase: Purification, kinetics and physical properties
    • Krista M. J. and Fonda M. L. (1973) Beef brain cytoplasmic aspartate aminotransferase: purification, kinetics and physical properties. Biochim. biophys. Acta 309, 83-96.
    • (1973) Biochim. Biophys. Acta , vol.309 , pp. 83-96
    • Krista, M.J.1    Fonda, M.L.2
  • 20
    • 0004015025 scopus 로고
    • E. & F. N. Spon Ltd, London
    • Long C. (1961) Biochemist's Handbook, p. 41. E. & F. N. Spon Ltd, London.
    • (1961) Biochemist's Handbook , pp. 41
    • Long, C.1
  • 21
    • 0015247072 scopus 로고
    • Molecular properties of the multiple aspartate aminotransferases purified from rat brain
    • Magee S. C. and Phillips A. T. (1971) Molecular properties of the multiple aspartate aminotransferases purified from rat brain. Biochemistry 10, 3397-3405.
    • (1971) Biochemistry , vol.10 , pp. 3397-3405
    • Magee, S.C.1    Phillips, A.T.2
  • 22
  • 23
    • 0011842380 scopus 로고
    • Aspartate aminotransferases from ribbed mussel gill tissue: Reactivity with β-L-cysteinesulfinic acid and other properties
    • McCormick A., Paynter K. T., Brodey M. M. and Bishop S. H. (1986) Aspartate aminotransferases from ribbed mussel gill tissue: reactivity with β-L-cysteinesulfinic acid and other properties. Comp. Biochem. Physiol. 84B, 163-166.
    • (1986) Comp. Biochem. Physiol. , vol.84 B , pp. 163-166
    • McCormick, A.1    Paynter, K.T.2    Brodey, M.M.3    Bishop, S.H.4
  • 24
    • 0014961286 scopus 로고
    • The isozymes of glutamate-aspartate transaminase. Mechanism of inhibition by dicarboxylic acids
    • Michuda C. M. and Martinez-Camon M. (1970) The isozymes of glutamate-aspartate transaminase. Mechanism of inhibition by dicarboxylic acids. J. biol. Chem. 245, 262-269.
    • (1970) J. Biol. Chem. , vol.245 , pp. 262-269
    • Michuda, C.M.1    Martinez-Camon, M.2
  • 25
    • 0001327546 scopus 로고
    • Amino acid transport and interconversions in tissues of freshly caught and food-deprived plaice Pleuronectes platessa L
    • Moon T. W. and Johnston I. A. (1981) Amino acid transport and interconversions in tissues of freshly caught and food-deprived plaice Pleuronectes platessa L. J. Fish Biol. 19, 653-663.
    • (1981) J. Fish Biol. , vol.19 , pp. 653-663
    • Moon, T.W.1    Johnston, I.A.2
  • 26
    • 0017412143 scopus 로고
    • Large-scale preparation of cytosolic and mitochondrial aspartate aminotransferases from pig heart
    • Morino Y., Tanase S., Watanabe T., Kagamiyama H. and Wada H. (1977) Large-scale preparation of cytosolic and mitochondrial aspartate aminotransferases from pig heart. J. Biochem. 82, 847-852.
    • (1977) J. Biochem. , vol.82 , pp. 847-852
    • Morino, Y.1    Tanase, S.2    Watanabe, T.3    Kagamiyama, H.4    Wada, H.5
  • 27
    • 0013956307 scopus 로고
    • Multiple forms of lactate dehydrogenase and aspartate aminotransferase in herring (Clupea harengus harengus L.)
    • Odense P. H., Allen T. M. and Leung T. C. (1966) Multiple forms of lactate dehydrogenase and aspartate aminotransferase in herring (Clupea harengus harengus L.). Can. J. Biochem. 44, 1319-1326.
    • (1966) Can. J. Biochem. , vol.44 , pp. 1319-1326
    • Odense, P.H.1    Allen, T.M.2    Leung, T.C.3
  • 28
    • 0011848425 scopus 로고
    • A sensitive and simple method for the determination of aspartate aminotransferase isoenzymes
    • London 1977, Karger, Basel
    • Ojala, K. and Konttinen, A. (1978) A sensitive and simple method for the determination of aspartate aminotransferase isoenzymes. In Enzymes in Health and Disease, Inaug. Scient. Meet. Int. Soc. Clin. Enzymol., London 1977, pp. 118-122. Karger, Basel.
    • (1978) Enzymes in Health and Disease, Inaug. Scient. Meet. Int. Soc. Clin. Enzymol. , pp. 118-122
    • Ojala, K.1    Konttinen, A.2
  • 29
    • 0016337394 scopus 로고
    • Purification and properties of dolphin muscle aspartate and alanine transaminases and their possible roles in the energy metabolism of diving mammals
    • Owen T. G. and Hochachka P. W. (1974) Purification and properties of dolphin muscle aspartate and alanine transaminases and their possible roles in the energy metabolism of diving mammals. Biochem. J. 143, 541-553.
    • (1974) Biochem. J. , vol.143 , pp. 541-553
    • Owen, T.G.1    Hochachka, P.W.2
  • 30
    • 0025108644 scopus 로고
    • Aspartate aminotransferase isoenzymes
    • Panteghini M. (1990) Aspartate aminotransferase isoenzymes.. Clin. Biochem. 23, 311-319.
    • (1990) Clin. Biochem. , vol.23 , pp. 311-319
    • Panteghini, M.1
  • 31
    • 84986451835 scopus 로고
    • Partial characterization of the cytosolic and mitochondrial aspartate aminotransferase from ribbed mussel gill tissue
    • Paynter K. T., Hoffmann R. J., Ellis L. L. and Bishop S. H. (1984) Partial characterization of the cytosolic and mitochondrial aspartate aminotransferase from ribbed mussel gill tissue. J. exp. Zool. 231, 185-197.
    • (1984) J. Exp. Zool. , vol.231 , pp. 185-197
    • Paynter, K.T.1    Hoffmann, R.J.2    Ellis, L.L.3    Bishop, S.H.4
  • 32
    • 0027931580 scopus 로고
    • Isolation and properties of mitochondrial aspartate aminotransferase from red muscle of grey mullet, Mugil auratus Risso
    • Petrović S., Krajnović-Ozretić M. and Ozretić B. (1994) Isolation and properties of mitochondrial aspartate aminotransferase from red muscle of grey mullet, Mugil auratus Risso. Biochim. biophys. Acta 1207, 201-207.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 201-207
    • Petrović, S.1    Krajnović-Ozretić, M.2    Ozretić, B.3
  • 35
    • 0018136952 scopus 로고
    • Aspartate aminotransferase activity and isoenzymes proportions in human liver tissues
    • Rej R. (1978) Aspartate aminotransferase activity and isoenzymes proportions in human liver tissues. Clin. Chem. 24, 1971-1979.
    • (1978) Clin. Chem. , vol.24 , pp. 1971-1979
    • Rej, R.1
  • 36
    • 0019513112 scopus 로고
    • Multiple molecular forms of human cytoplasmic aspartate aminotransferase
    • Rej R. (1981) Multiple molecular forms of human cytoplasmic aspartate aminotransferase. Clin. chim. Acta 112, 1-11.
    • (1981) Clin. Chim. Acta , vol.112 , pp. 1-11
    • Rej, R.1
  • 37
    • 0015919543 scopus 로고
    • Mitochondrial-cytosolic interactions in perfused rat heart
    • Safer B. and Williamson J. R. (1973) Mitochondrial-cytosolic interactions in perfused rat heart. J. biol. Chem. 248, 2570-2579.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2570-2579
    • Safer, B.1    Williamson, J.R.2
  • 38
    • 0015935347 scopus 로고
    • Simultaneous isolation and characterization of chicken supernatant and mitochondrial isoenzymes of aspartate transaminase
    • Shrawder E. J. and Martinez-Carrion M. (1973) Simultaneous isolation and characterization of chicken supernatant and mitochondrial isoenzymes of aspartate transaminase. J. biol. Chem. 248, 2140-2146.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2140-2146
    • Shrawder, E.J.1    Martinez-Carrion, M.2
  • 39
    • 0018246101 scopus 로고
    • Cytosolic and mitochondrial isoenzymes of glutamic-oxalacetic transaminase from human heart
    • Teranishi H., Kagamiyama H., Teranishi K., Wada H., Yamano T. and Morino Y. (1978) Cytosolic and mitochondrial isoenzymes of glutamic-oxalacetic transaminase from human heart. J. biol. Chem. 253, 8842-8847.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8842-8847
    • Teranishi, H.1    Kagamiyama, H.2    Teranishi, K.3    Wada, H.4    Yamano, T.5    Morino, Y.6
  • 40
    • 0015923590 scopus 로고
    • Genetic variation of mitochondrial aspartate aminotransferase in the teleost Cyprinodon nevadensis
    • Turner B. J. (1973) Genetic variation of mitochondrial aspartate aminotransferase in the teleost Cyprinodon nevadensis. Comp. Biochem. Physiol. 44B, 89-92.
    • (1973) Comp. Biochem. Physiol. , vol.44 B , pp. 89-92
    • Turner, B.J.1
  • 41
    • 0024833851 scopus 로고
    • Free amino acid profiles of aerobic (red) and anaerobic (white) skeletal muscle of the cyprinid fish Carassius auratus L. (goldfish)
    • Van der Boon J., Van den Thillart G. E. E. J. M. and Addink A. D. F. (1989) Free amino acid profiles of aerobic (red) and anaerobic (white) skeletal muscle of the cyprinid fish Carassius auratus L. (goldfish). Comp. Biochem. Physiol. 94A, 809-812.
    • (1989) Comp. Biochem. Physiol. , vol.94 A , pp. 809-812
    • Van Der Boon, J.1    Van Den Thillart, G.E.E.J.M.2    Addink, A.D.F.3
  • 42
    • 0000427037 scopus 로고
    • A kinetic and equilibrium analysis of the glutamic oxaloacetate transaminase mechanism
    • Velick S. F. and Vavra J. (1962) A kinetic and equilibrium analysis of the glutamic oxaloacetate transaminase mechanism. J. biol. Chem. 237, 2109-2122.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2109-2122
    • Velick, S.F.1    Vavra, J.2
  • 43
    • 0002395357 scopus 로고
    • Aspects of intermediary metabolism in salmonid fish
    • Walton M. J. and Cowey C. B. (1982) Aspects of intermediary metabolism in salmonid fish. Comp. Biochem. Physiol. 73B, 59-79.
    • (1982) Comp. Biochem. Physiol. , vol.73 B , pp. 59-79
    • Walton, M.J.1    Cowey, C.B.2
  • 44
    • 0018372036 scopus 로고
    • Generation of aspartate aminotransferase multiple forms by deamination
    • Williams J. A. and John R. A. (1979) Generation of aspartate aminotransferase multiple forms by deamination. Biochem. J. 177, 121-127.
    • (1979) Biochem. J. , vol.177 , pp. 121-127
    • Williams, J.A.1    John, R.A.2
  • 45
    • 0018802745 scopus 로고
    • Cysteine sulfinate transamination activity of aspartate aminotransferases
    • Yagi T., Kagamiyama H. and Nozaki M. (1979) Cysteine sulfinate transamination activity of aspartate aminotransferases. Biochem. biophys. Res. Commun. 90, 447-452.
    • (1979) Biochem. Biophys. Res. Commun. , vol.90 , pp. 447-452
    • Yagi, T.1    Kagamiyama, H.2    Nozaki, M.3
  • 46
    • 0019467908 scopus 로고
    • A sensitive method for the detection of aspartate: 2-oxoglutarate aminotransferase activity on polyacrylamide gels
    • Yagi T., Kagamiyama H. and Nozaki M. (1981) A sensitive method for the detection of aspartate: 2-oxoglutarate aminotransferase activity on polyacrylamide gels. Analyt. Biochem. 110, 146-149.
    • (1981) Analyt. Biochem. , vol.110 , pp. 146-149
    • Yagi, T.1    Kagamiyama, H.2    Nozaki, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.