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Volumn 37, Issue 10, 1999, Pages 731-739

Purification and characterization of two glutamate dehydrogenase isoenzymes from Brassica napus

Author keywords

Brassica napus; Characterization; Glutamate dehydrogenase; Localization; Purification

Indexed keywords

2 OXOGLUTARIC ACID; AMMONIA; CELL FRACTIONATION; ELECTROPHORETIC MOBILITY; ENZYME PURIFICATION; GLUTAMATE DEHYDROGENASE; ISOENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PLANT PRODUCT;

EID: 0032758990     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0981-9428(00)86686-3     Document Type: Article
Times cited : (5)

References (35)
  • 1
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts, Phenoloxidase in Beta vulgaris
    • Arnon D. Copper enzymes in isolated chloroplasts, Phenoloxidase in Beta vulgaris. Plant Physiol. 24:1949;1-15.
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.1
  • 2
    • 0344730422 scopus 로고
    • Studies on nitrite reductase in barley
    • Bourne W.F., Miflin B.J. Studies on nitrite reductase in barley. Planta. 111:1973;47-56.
    • (1973) Planta , vol.111 , pp. 47-56
    • Bourne, W.F.1    Miflin, B.J.2
  • 3
    • 0001031722 scopus 로고
    • A study of the role of glutamate dehydrogenase in the nitrogen metabolism of Arabidopsis thaliana
    • Cammaerts D., Jacobs M. A study of the role of glutamate dehydrogenase in the nitrogen metabolism of Arabidopsis thaliana. Planta. 163:1985;517-526.
    • (1985) Planta , vol.163 , pp. 517-526
    • Cammaerts, D.1    Jacobs, M.2
  • 4
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum proteins
    • Davis B.J. Disc electrophoresis. II. Method and application to human serum proteins. Ann. N. Y. Acad. Sci. 121:1964;119-128.
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , pp. 119-128
    • Davis, B.J.1
  • 5
    • 0345160701 scopus 로고
    • La glutamate deshydrogénase de la luzerne: Aspects cytologiques, structuraux et évolutifs
    • de Vienne D. La glutamate deshydrogénase de la luzerne: aspects cytologiques, structuraux et évolutifs. Can. J. Genet. Cytol. 25:1983;146-160.
    • (1983) Can. J. Genet. Cytol. , vol.25 , pp. 146-160
    • De Vienne, D.1
  • 6
    • 0344730417 scopus 로고
    • The isozymic nature and kinetic properties of glutamate dehydrogenase from safflower seedlings
    • Erell A., Mor H., Barash I. The isozymic nature and kinetic properties of glutamate dehydrogenase from safflower seedlings. Plant Cell Physiol. 14:1973;39-50.
    • (1973) Plant Cell Physiol. , vol.14 , pp. 39-50
    • Erell, A.1    Mor, H.2    Barash, I.3
  • 8
    • 0345592691 scopus 로고
    • Role of mitochondorial glutamate dehydrogenase in the reassimilation of ammonia produced by glycine serine transformation
    • Hartmann T., Ehmke A. Role of mitochondorial glutamate dehydrogenase in the reassimilation of ammonia produced by glycine serine transformation. Planta. 149:1980;207-208.
    • (1980) Planta , vol.149 , pp. 207-208
    • Hartmann, T.1    Ehmke, A.2
  • 9
    • 38249032379 scopus 로고
    • Purification and properties of NAD-glutamate dehydrogenase from turnip mitochondria
    • Itagaki T., Dry I.B., Wiskich J.T. Purification and properties of NAD-glutamate dehydrogenase from turnip mitochondria. Phytochemistry. 27:1988;3373-3378.
    • (1988) Phytochemistry , vol.27 , pp. 3373-3378
    • Itagaki, T.1    Dry, I.B.2    Wiskich, J.T.3
  • 11
    • 0345160700 scopus 로고
    • The effect of light and exogenously supplied ammonium ions on glutamate dehydrogenase activity and isoforms in young mustard (Sinapis alba L.) seedling
    • Lettgen L., Britsch L., Kasemir H. The effect of light and exogenously supplied ammonium ions on glutamate dehydrogenase activity and isoforms in young mustard (Sinapis alba L.) seedling. Bot. Acta. 102:1989;189-195.
    • (1989) Bot. Acta , vol.102 , pp. 189-195
    • Lettgen, L.1    Britsch, L.2    Kasemir, H.3
  • 12
    • 0000837713 scopus 로고
    • Intracellular localization and properties of NADH-glutamate dehydrogenase from Vitis vinifera L.: Purification and characterization of the major leaf isoenzyme
    • Loulakakis C.A., Roubelakis-Angelakis K.A. Intracellular localization and properties of NADH-glutamate dehydrogenase from Vitis vinifera L.: purification and characterization of the major leaf isoenzyme. J. Exp. Bot. 41:1990;1223-1230.
    • (1990) J. Exp. Bot. , vol.41 , pp. 1223-1230
    • Loulakakis, C.A.1    Roubelakis-Angelakis, K.A.2
  • 13
    • 0001446787 scopus 로고
    • Plant NAD(H)-glutamate dehydrogenase consists of two subunit polypeptides and their participation in the seven isoenzymes occurs in an ordered ratio
    • Loulakakis K.A., Roubelakis-Angelakis K.A. Plant NAD(H)-glutamate dehydrogenase consists of two subunit polypeptides and their participation in the seven isoenzymes occurs in an ordered ratio. Plant Physiol. 97:1991;104-111.
    • (1991) Plant Physiol. , vol.97 , pp. 104-111
    • Loulakakis, K.A.1    Roubelakis-Angelakis, K.A.2
  • 14
    • 0030062030 scopus 로고    scopus 로고
    • The seven NAD(H)-glutamate dehydrogenase isoenzymes exhibit similar anabolic and catabolic activities
    • Loulakakis K.A., Roubelakis-Angelakis K.A. The seven NAD(H)-glutamate dehydrogenase isoenzymes exhibit similar anabolic and catabolic activities. Physiol. Plant. 96:1996;29-35.
    • (1996) Physiol. Plant. , vol.96 , pp. 29-35
    • Loulakakis, K.A.1    Roubelakis-Angelakis, K.A.2
  • 15
    • 0031783607 scopus 로고    scopus 로고
    • Pollen-specific glutamate dehydrogenase (GDH II) is observed after microspore mitosis in Capsicum annuum L.
    • Manoharan M., Rudramuniyappa C.K. Pollen-specific glutamate dehydrogenase (GDH II) is observed after microspore mitosis in Capsicum annuum L. J. Plant Physiol. 152:1998;586-588.
    • (1998) J. Plant Physiol. , vol.152 , pp. 586-588
    • Manoharan, M.1    Rudramuniyappa, C.K.2
  • 16
    • 0030029406 scopus 로고    scopus 로고
    • Arabidopsis mutant analysis and gene regulation define a nonredundant role for glutamate dehydrogenase in nitrogen assimilation
    • Melo-Oliveira R., Oliveira I.G., Coruzzi G.M. Arabidopsis mutant analysis and gene regulation define a nonredundant role for glutamate dehydrogenase in nitrogen assimilation. Proc. Natl. Acad. Sci. USA. 93:1996;4718-4723.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4718-4723
    • Melo-Oliveira, R.1    Oliveira, I.G.2    Coruzzi, G.M.3
  • 17
    • 0019012524 scopus 로고
    • Glutamate dehydrogenase from Medicago sativa L.: Purification and comparative kinetic studies of organ-specific multiple forms
    • Nagel M., Hartmann T. Glutamate dehydrogenase from Medicago sativa L.: Purification and comparative kinetic studies of organ-specific multiple forms. Z. Naturforsch. 35c:1980;406-415.
    • (1980) Z. Naturforsch. , vol.35 , pp. 406-415
    • Nagel, M.1    Hartmann, T.2
  • 18
    • 0031281306 scopus 로고    scopus 로고
    • Regulation of peanut glutamate dehydrogenase by methionine sulphoximine
    • Osuji G.O., Madu W.C. Regulation of peanut glutamate dehydrogenase by methionine sulphoximine. Phytochemistry. 46:1997;817-825.
    • (1997) Phytochemistry , vol.46 , pp. 817-825
    • Osuji, G.O.1    Madu, W.C.2
  • 19
    • 0014985066 scopus 로고
    • Glutamate dehydrogenase from pea roots: Purification and properties of the enzyme
    • Pahlich E., Joy K.W. Glutamate dehydrogenase from pea roots: Purification and properties of the enzyme. Can. J. Biochem. 49:1971;127-138.
    • (1971) Can. J. Biochem. , vol.49 , pp. 127-138
    • Pahlich, E.1    Joy, K.W.2
  • 21
    • 0015504296 scopus 로고
    • Identification and properties of an inducible manokase from Streptomyces violaceoruber
    • Sabater B., Sebastián J., Asensio C. Identification and properties of an inducible manokase from Streptomyces violaceoruber. Biochim. Biophys. Acta. 284:1972;406-413.
    • (1972) Biochim. Biophys. Acta , vol.284 , pp. 406-413
    • Sabater, B.1    Sebastián, J.2    Asensio, C.3
  • 22
    • 0018990321 scopus 로고
    • Plant NAD-glutamate dehydrogenase. Purification, molecular properties and metal ion activation of the enzymes from Lemma minor and Pisum sativum
    • Scheid H.W., Ehmke A., Hartmann T. Plant NAD-glutamate dehydrogenase. Purification, molecular properties and metal ion activation of the enzymes from Lemma minor and Pisum sativum. Z. Naturforsch. 35c:1980;213-221.
    • (1980) Z. Naturforsch. , vol.35 , pp. 213-221
    • Scheid, H.W.1    Ehmke, A.2    Hartmann, T.3
  • 23
    • 0013305829 scopus 로고
    • Separation of plant isozymes, peroxidase, by isoelectronic gel electrophoresis
    • Sekine M., Kawaoka A., Shinmyo A. Separation of plant isozymes, peroxidase, by isoelectronic gel electrophoresis. Plant Cell Technol. 6:1994;67-71.
    • (1994) Plant Cell Technol. , vol.6 , pp. 67-71
    • Sekine, M.1    Kawaoka, A.2    Shinmyo, A.3
  • 24
    • 0001141677 scopus 로고
    • Role and regulation of L-glutamate dehydrogenase activity in higher plant
    • Srivastava H.S., Singh R.P. Role and regulation of L-glutamate dehydrogenase activity in higher plant. Phytochemistry. 26:1987;597-610.
    • (1987) Phytochemistry , vol.26 , pp. 597-610
    • Srivastava, H.S.1    Singh, R.P.2
  • 25
    • 0344298283 scopus 로고
    • Properties of glutamate dehydrogenase purified from green tobacco tissue
    • Takahashi Y., Furuhashi K. Properties of glutamate dehydrogenase purified from green tobacco tissue. Plant Cell Physiol. 21:1980;1067-1075.
    • (1980) Plant Cell Physiol. , vol.21 , pp. 1067-1075
    • Takahashi, Y.1    Furuhashi, K.2
  • 26
    • 0029767554 scopus 로고    scopus 로고
    • Purification of mitochondrial glutamate dehydrogenase from dark-grown soybean seedlings
    • Turano F., Dashner R., Upadhyaya A., Caldwell C.R. Purification of mitochondrial glutamate dehydrogenase from dark-grown soybean seedlings. Plant Physiol. 112:1996;1357-1364.
    • (1996) Plant Physiol. , vol.112 , pp. 1357-1364
    • Turano, F.1    Dashner, R.2    Upadhyaya, A.3    Caldwell, C.R.4
  • 27
    • 0031127224 scopus 로고    scopus 로고
    • Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis
    • Turano F.J., Thakkar S.S., Fang T., Weisemann J.M. Characterization and expression of NAD(H)-dependent glutamate dehydrogenase genes in Arabidopsis. Plant Physiol. 113:1997;1329-1341.
    • (1997) Plant Physiol. , vol.113 , pp. 1329-1341
    • Turano, F.J.1    Thakkar, S.S.2    Fang, T.3    Weisemann, J.M.4
  • 28
    • 0031783212 scopus 로고    scopus 로고
    • Senescence development of Brassica napus leaf protoplast during isolation and subsequent culture
    • Watanabe M., Kawasaki H., Itho Y., Watanabe Y. Senescence development of Brassica napus leaf protoplast during isolation and subsequent culture. J. Plant Physiol. 152:1998;487-493.
    • (1998) J. Plant Physiol. , vol.152 , pp. 487-493
    • Watanabe, M.1    Kawasaki, H.2    Itho, Y.3    Watanabe, Y.4
  • 29
    • 84989738103 scopus 로고
    • Induction of a specific isoenzyme of glutamate dehydrogenase during isolation and the first 48h of culture of Brassica napus leaf protoplasts
    • Watanabe M., Nakayama H., Watanabe Y., Shimada N. Induction of a specific isoenzyme of glutamate dehydrogenase during isolation and the first 48h of culture of Brassica napus leaf protoplasts. Physiol. Plant. 86:1992;231-235.
    • (1992) Physiol. Plant. , vol.86 , pp. 231-235
    • Watanabe, M.1    Nakayama, H.2    Watanabe, Y.3    Shimada, N.4
  • 30
    • 0028115389 scopus 로고
    • Mechanical slicing-induced alteration of GDH isoenzyme patterns in Brassica napus leaf protoplasts
    • Watanabe M., Nakayama H., Watanabe Y., Shimada N. Mechanical slicing-induced alteration of GDH isoenzyme patterns in Brassica napus leaf protoplasts. J. Plant Physiol. 143:1994;87-91.
    • (1994) J. Plant Physiol. , vol.143 , pp. 87-91
    • Watanabe, M.1    Nakayama, H.2    Watanabe, Y.3    Shimada, N.4
  • 31
    • 0001685934 scopus 로고
    • Synthesis of glutamate by mitochondria - An anaplerotic function for glutamate dehydrogenase
    • Yamaya T., Oaks A. Synthesis of glutamate by mitochondria - An anaplerotic function for glutamate dehydrogenase. Physiol. Plant. 70:1987;749-756.
    • (1987) Physiol. Plant. , vol.70 , pp. 749-756
    • Yamaya, T.1    Oaks, A.2
  • 32
    • 84950014120 scopus 로고
    • Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots
    • Yamaya T.Y., Oaks A., Matsumoto H. Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots. Plant Physiol. 76:1984;1009-1013.
    • (1984) Plant Physiol. , vol.76 , pp. 1009-1013
    • Yamaya, T.Y.1    Oaks, A.2    Matsumoto, H.3
  • 33
    • 0001694058 scopus 로고
    • Freezing injury and phospholipid degradation in vitro in woody plant cells
    • Yoshida S. Freezing injury and phospholipid degradation in vitro in woody plant cells. Plant Physiol. 64:1979;241-246.
    • (1979) Plant Physiol. , vol.64 , pp. 241-246
    • Yoshida, S.1
  • 34
    • 0344730413 scopus 로고
    • Isoenzymes of glutamate dehydrogenase in plants
    • Yue S.B. Isoenzymes of glutamate dehydrogenase in plants. Plant Physiol. 44:1969;453-457.
    • (1969) Plant Physiol. , vol.44 , pp. 453-457
    • Yue, S.B.1
  • 35
    • 0001398314 scopus 로고
    • The use of fura-2 fluorescence to monitor the movement of free calcium ions into the matrix of plant mitochondria (Pisum sativum and Helianthus tuberosus)
    • Zottini M., Zannoni D. The use of fura-2 fluorescence to monitor the movement of free calcium ions into the matrix of plant mitochondria (Pisum sativum and Helianthus tuberosus). Plant Physiol. 102:1993;573-578.
    • (1993) Plant Physiol. , vol.102 , pp. 573-578
    • Zottini, M.1    Zannoni, D.2


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