메뉴 건너뛰기




Volumn 96, Issue 1, 1996, Pages 29-35

The seven NAD(H)-glutamate dehydrogenase isoenzymes exhibit similar anabolic and catabolic activities

Author keywords

Ammonia assimilation; Glutamate dehydrogenase; Grapevine; Nitrogen metabolism; Vitis vinifera

Indexed keywords

VITIS VINIFERA;

EID: 0030062030     PISSN: 00319317     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3054.1996.tb00179.x     Document Type: Article
Times cited : (58)

References (23)
  • 1
    • 0018234762 scopus 로고
    • Genetic variation in natural populations of wild barley (Hordeum spontaneum)
    • Brown, A. H. D., Nevo, E., Zohary, D. & Dagan, O. 1978. Genetic variation in natural populations of wild barley (Hordeum spontaneum). - Genetica 49: 97-108.
    • (1978) Genetica , vol.49 , pp. 97-108
    • Brown, A.H.D.1    Nevo, E.2    Zohary, D.3    Dagan, O.4
  • 2
    • 0019964983 scopus 로고
    • Purification and genetic control of NAD-dependent glutamate dehydrogenase from Drosophila melanogaster
    • Caggese, C., De Pinto, V. & Ferrendino, A. 1982. Purification and genetic control of NAD-dependent glutamate dehydrogenase from Drosophila melanogaster. - Biochem. Genet. 20: 449-460.
    • (1982) Biochem. Genet. , vol.20 , pp. 449-460
    • Caggese, C.1    De Pinto, V.2    Ferrendino, A.3
  • 3
    • 0001031722 scopus 로고
    • A study of the role of glutamate dehydrogenase in the nitrogen metabolism of Arabidopsis thaliana
    • Cammaerts, D. M. & Jacobs, M. 1985. A study of the role of glutamate dehydrogenase in the nitrogen metabolism of Arabidopsis thaliana. - Planta 163: 517-526.
    • (1985) Planta , vol.163 , pp. 517-526
    • Cammaerts, D.M.1    Jacobs, M.2
  • 4
    • 0010236620 scopus 로고
    • Malate: A possible source of error in the NAD glutamate dehydrogenase assay
    • Fricke, W. & Pahlich, E. 1992. Malate: a possible source of error in the NAD glutamate dehydrogenase assay. - J. Exp. Bot. 43: 1515-1518.
    • (1992) J. Exp. Bot. , vol.43 , pp. 1515-1518
    • Fricke, W.1    Pahlich, E.2
  • 5
    • 0026654155 scopus 로고
    • Staining for enzymatic activity after gel electrophoresis. I
    • Gabriel, O. & Gersten, D. M. 1992. Staining for enzymatic activity after gel electrophoresis. I. - Anal. Biochem. 203: 1-21.
    • (1992) Anal. Biochem. , vol.203 , pp. 1-21
    • Gabriel, O.1    Gersten, D.M.2
  • 6
    • 0001480763 scopus 로고
    • L-Malate. Bestimmung mit Malatdehydrogenase und NAD
    • (H. U. Bergmeyer, ed.), Verlag Chemie, Weinheim
    • Hohorst, H. M. 1970. L-Malate. Bestimmung mit Malatdehydrogenase und NAD. - In Methoden der Enzymatischen Analyse (H. U. Bergmeyer, ed.), Vol. II, pp. 1544-1548. Verlag Chemie, Weinheim.
    • (1970) Methoden der Enzymatischen Analyse , vol.2 , pp. 1544-1548
    • Hohorst, H.M.1
  • 7
    • 0008995971 scopus 로고
    • Changes in the levels of enzymes involved in ammonia assimilation during the development of Phaseolus vulgaris seedlings. Effects of exogenous ammonia
    • Leon, E., De La Haba, P. & Maldonado, J. M. 1990. Changes in the levels of enzymes involved in ammonia assimilation during the development of Phaseolus vulgaris seedlings. Effects of exogenous ammonia. - Physiol. Plant. 80: 20-26.
    • (1990) Physiol. Plant. , vol.80 , pp. 20-26
    • Leon, E.1    De La Haba, P.2    Maldonado, J.M.3
  • 8
    • 0000837713 scopus 로고
    • Intracellular localization and properties of NADH-glutamate dehydrogenase from Vitis vinifera L.: Purification and characterization of the major leaf isoenzyme
    • Loulakakis, K. A. & Roubelakis-Angelakis, K. A. 1990a. Intracellular localization and properties of NADH-glutamate dehydrogenase from Vitis vinifera L.: Purification and characterization of the major leaf isoenzyme. - J. Exp. Bot. 41: 1223-1230.
    • (1990) J. Exp. Bot. , vol.41 , pp. 1223-1230
    • Loulakakis, K.A.1    Roubelakis-Angelakis, K.A.2
  • 9
    • 0000639186 scopus 로고
    • Immunocharacterization of NADH-glutamate dehydrogenase from Vitis vinifera L.
    • _ & Roubelakis-Angelakis, K. A. 1990b. Immunocharacterization of NADH-glutamate dehydrogenase from Vitis vinifera L. - Plant Physiol. 94: 109-113.
    • (1990) Plant Physiol. , vol.94 , pp. 109-113
    • Roubelakis-Angelakis, K.A.1
  • 10
    • 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
    • _ & Roubelakis-Angelakis, K. A. 1991. 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: 104-111.
    • (1991) Plant Physiol. , vol.97 , pp. 104-111
    • Roubelakis-Angelakis, K.A.1
  • 11
    • 0001741796 scopus 로고
    • Ammonium-induced increase in NADH-glutamate dehydrogenase activity is caused by de novo synthesis of the α-subunit
    • _ & Roubelakis-Angelakis, K. A. 1992. Ammonium-induced increase in NADH-glutamate dehydrogenase activity is caused by de novo synthesis of the α-subunit. - Planta 187: 322-327.
    • (1992) Planta , vol.187 , pp. 322-327
    • Roubelakis-Angelakis, K.A.1
  • 12
    • 0028120207 scopus 로고
    • Regulation of glutamate dehydrogenase and glutamine synthetase in avocado fruit during development and ripening
    • _ , Roubelakis-Angelakis, K. A. & Kanellis, A. K. 1994. Regulation of glutamate dehydrogenase and glutamine synthetase in avocado fruit during development and ripening. - Plant Physiol. 106: 217-222.
    • (1994) Plant Physiol. , vol.106 , pp. 217-222
    • Roubelakis-Angelakis, K.A.1    Kanellis, A.K.2
  • 14
    • 0000007524 scopus 로고
    • Differential role of glutamate dehydrogenase in nitrogen metabolism of maize tissues
    • Loyola-Vargas, V. M. & de Jimenez, E. S. 1984. Differential role of glutamate dehydrogenase in nitrogen metabolism of maize tissues. - Plant Physiol. 76: 536-540.
    • (1984) Plant Physiol. , vol.76 , pp. 536-540
    • Loyola-Vargas, V.M.1    De Jimenez, E.S.2
  • 16
    • 0007746576 scopus 로고
    • Glutamate dehydrogenase activity and assimilation of inorganic nitrogen in maize seedlings
    • Singh, R. P. & Srivastava, H. S. 1982. Glutamate dehydrogenase activity and assimilation of inorganic nitrogen in maize seedlings. - Biochem. Physiol. Pflanz. 177: 633-642.
    • (1982) Biochem. Physiol. Pflanz. , vol.177 , pp. 633-642
    • Singh, R.P.1    Srivastava, H.S.2
  • 17
    • 0348023685 scopus 로고
    • Regulation of glutamate dehydrogenase activity by amino acids in maize seedlings
    • _ & Srivastava, H. S. 1983. Regulation of glutamate dehydrogenase activity by amino acids in maize seedlings. - Physiol. Plant. 57: 549-554.
    • (1983) Physiol. Plant. , vol.57 , pp. 549-554
    • Srivastava, H.S.1
  • 18
    • 0001141677 scopus 로고
    • Role and regulation of L-glutamate dehydrogenase activity in higher plants
    • Srivastava, H. S. & Singh, R. P. 1987. Role and regulation of L-glutamate dehydrogenase activity in higher plants. - Phytochemistry 26: 597-610.
    • (1987) Phytochemistry , vol.26 , pp. 597-610
    • Srivastava, H.S.1    Singh, R.P.2
  • 19
    • 0030070662 scopus 로고    scopus 로고
    • The amino acid sequence similarity of plant glutamate dehydrogenase to the extremophilic archaeal enzyme conforms to its stress-related function
    • In press
    • Syntichaki, K. A., Loulakakis, K. A. & Roubelakis-Angelakis, K. A. 1996. The amino acid sequence similarity of plant glutamate dehydrogenase to the extremophilic archaeal enzyme conforms to its stress-related function. - Gene (In press).
    • (1996) Gene
    • Syntichaki, K.A.1    Loulakakis, K.A.2    Roubelakis-Angelakis, K.A.3
  • 20
    • 33747379226 scopus 로고
    • Enzyme activity staining
    • (S. D. Tanksley and T. J. Orton, eds), Elsevier Science Publishers B. V., Amsterdam. ISBN 0-444-42226-9
    • Vallejos, E. 1983. Enzyme activity staining. - In Isozymes in Plant Genetics and Breeding (S. D. Tanksley and T. J. Orton, eds), Part A, pp. 469-516. Elsevier Science Publishers B. V., Amsterdam. ISBN 0-444-42226-9.
    • (1983) Isozymes in Plant Genetics and Breeding , Issue.PART A , pp. 469-516
    • Vallejos, E.1
  • 21
    • 84989738103 scopus 로고
    • Induction of a specific isoenzyme of glutamate dehydrogenase during isolation and the first 48 h of culture of Brassica napus leaf protoplasts
    • Watanabe, M., Nakayama, H., Watanabe, Y. & Shimada, N. 1992. Induction of a specific isoenzyme of glutamate dehydrogenase during isolation and the first 48 h of culture of Brassica napus leaf protoplasts. - Physiol. Plant. 86: 231-235.
    • (1992) Physiol. Plant. , vol.86 , pp. 231-235
    • Watanabe, M.1    Nakayama, H.2    Watanabe, Y.3    Shimada, N.4
  • 22
    • 0028115389 scopus 로고
    • Mechanical slicing-induced alteration of GDH isoenzyme patterns in Brassica napus leaf protoplasts
    • _ , Nakayama, H., Watanabe, Y. & Shimada, N. 1994. Mechanical slicing-induced alteration of GDH isoenzyme patterns in Brassica napus leaf protoplasts. - J. Plant Physiol. 143: 87-91.
    • (1994) J. Plant Physiol. , vol.143 , pp. 87-91
    • Nakayama, H.1    Watanabe, Y.2    Shimada, N.3
  • 23
    • 84950014120 scopus 로고
    • Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots
    • Yamaya, T., Oaks, A. & Matsumoto, H. 1984. Characteristics of glutamate dehydrogenase in mitochondria prepared from corn shoots. - Plant Physiol. 76: 1009-1013.
    • (1984) Plant Physiol. , vol.76 , pp. 1009-1013
    • Yamaya, T.1    Oaks, A.2    Matsumoto, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.