메뉴 건너뛰기




Volumn 207, Issue 2, 1998, Pages 280-285

Plant NADP-dependent isocitrate dehydrogenases are predominantly localized in the cytosol

Author keywords

Ketoglutarate; Chloroplast; Cytosol; Isocitrate dehydrogenase; Isoenzyme pattern

Indexed keywords

2 OXOGLUTARIC ACID; CHLOROPLAST; ENZYME LOCALIZATION; IMMUNOLOGICAL TECHNIQUE; ION EXCHANGE CHROMATOGRAPHY; ISOCITRATE DEHYDROGENASE; ISOENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; NITROGEN FIXATION; PLANT PRODUCT; PROTEIN DETECTION;

EID: 0032422614     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250050484     Document Type: Article
Times cited : (45)

References (23)
  • 1
    • 0028005597 scopus 로고
    • Characterization of a mitochondrial NADP-dependent isocitrate dehydrogenase in axis of germinating sunflower seeds
    • Attucci S, Rivoal J, Brouquisse R, Carde JP, Pradet A, Raymond P (1994) Characterization of a mitochondrial NADP-dependent isocitrate dehydrogenase in axis of germinating sunflower seeds. Plant Sci 102: 49-59
    • (1994) Plant Sci , vol.102 , pp. 49-59
    • Attucci, S.1    Rivoal, J.2    Brouquisse, R.3    Carde, J.P.4    Pradet, A.5    Raymond, P.6
  • 2
    • 84980184968 scopus 로고
    • The quantitative analysis of chlorophyll a and b in plant extracts
    • Bruisma J (1963) The quantitative analysis of chlorophyll a and b in plant extracts. Photochem Photobiol 2: 241-249
    • (1963) Photochem Photobiol , vol.2 , pp. 241-249
    • Bruisma, J.1
  • 3
    • 0000518813 scopus 로고
    • Do the mitochondria provide the 2-oxoglutarate needed for glutamate synthesis in higher plants?
    • Chen RD, Gadal P (1990a) Do the mitochondria provide the 2-oxoglutarate needed for glutamate synthesis in higher plants? Plant Physiol Biochem 28: 141-145
    • (1990) Plant Physiol Biochem , vol.28 , pp. 141-145
    • Chen, R.D.1    Gadal, P.2
  • 4
    • 0000980429 scopus 로고
    • Structure, functions and regulation of NAD and NADP dependent isocitrate dehydrogenases in higher plants and in other organisms
    • Chen RD, Gadal P (1990b) Structure, functions and regulation of NAD and NADP dependent isocitrate dehydrogenases in higher plants and in other organisms. Plant Physiol Biochem 28: 411-427
    • (1990) Plant Physiol Biochem , vol.28 , pp. 411-427
    • Chen, R.D.1    Gadal, P.2
  • 5
    • 0024288496 scopus 로고
    • Purification and comparative properties of the cytosolic isocitrate dehydrogenase (NADP) from pea (Pisum sativum) roots and leaves
    • Chen RD, Le Marechal P, Vidal J, Gadal P (1988) Purification and comparative properties of the cytosolic isocitrate dehydrogenase (NADP) from pea (Pisum sativum) roots and leaves. Eur J Biochem 175: 565-572
    • (1988) Eur J Biochem , vol.175 , pp. 565-572
    • Chen, R.D.1    Le Marechal, P.2    Vidal, J.3    Gadal, P.4
  • 6
    • 0004881952 scopus 로고
    • Chromatographic and immunological evidence that chloroplastic and cytosolic pea leaf NADP-isocitrate dehydrogenases are distinct isoenzymes
    • Chen RD, Bismuth E, Champigny ML, Gadal P (1989) Chromatographic and immunological evidence that chloroplastic and cytosolic pea leaf NADP-isocitrate dehydrogenases are distinct isoenzymes. Planta 178: 157-163
    • (1989) Planta , vol.178 , pp. 157-163
    • Chen, R.D.1    Bismuth, E.2    Champigny, M.L.3    Gadal, P.4
  • 7
    • 0030057614 scopus 로고    scopus 로고
    • +-dependent isocitrate dehydrogenases in mitochondria purified from Picea abies seedlings
    • +-dependent isocitrate dehydrogenases in mitochondria purified from Picea abies seedlings. Physiol Plant 96: 312-318
    • (1996) Physiol Plant , vol.96 , pp. 312-318
    • Cornu, S.1    Pireaux, J.C.2    Gerard, J.3    Dizengremel, P.4
  • 8
    • 0027205318 scopus 로고
    • Lack of aconitase in glyoxysomes and peroxisomes
    • Courtois-Verniquet F, Douce R (1993) Lack of aconitase in glyoxysomes and peroxisomes. Biochem J 294: 103-107
    • (1993) Biochem J , vol.294 , pp. 103-107
    • Courtois-Verniquet, F.1    Douce, R.2
  • 9
    • 0029137803 scopus 로고
    • Subcellular and developmental changes in distribution of aconitase isoforms in pumpkin cotyledons
    • De Bellis L, Hayashi M, Nishimura M, Alpi A (1995) Subcellular and developmental changes in distribution of aconitase isoforms in pumpkin cotyledons. Planta 195: 464-468
    • (1995) Planta , vol.195 , pp. 464-468
    • De Bellis, L.1    Hayashi, M.2    Nishimura, M.3    Alpi, A.4
  • 11
    • 0040271539 scopus 로고
    • Alpha-ketoglutarate supply for amino acid synthesis in higher plant chloroplasts
    • Elias BA, Givan CV (1977) Alpha-ketoglutarate supply for amino acid synthesis in higher plant chloroplasts. Plant Physiol 59: 738-740
    • (1977) Plant Physiol , vol.59 , pp. 738-740
    • Elias, B.A.1    Givan, C.V.2
  • 13
    • 0029111038 scopus 로고
    • Changes in NADP-linked isocitrate dehydrogenase during tomato fruit ripening
    • Gallardo F, Galvez S, Gadal P, Canovas (1995) Changes in NADP-linked isocitrate dehydrogenase during tomato fruit ripening. Planta 196: 148-154
    • (1995) Planta , vol.196 , pp. 148-154
    • Gallardo, F.1    Galvez, S.2    Gadal, P.3    Canovas4
  • 14
    • 0027972175 scopus 로고
    • Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mexotrophic tobacco cells
    • Galvez S, Bismuth E, Sarda C, Gadal P (1994) Purification and characterization of chloroplastic NADP-isocitrate dehydrogenase from mexotrophic tobacco cells. Plant Physiol 105: 593-600
    • (1994) Plant Physiol , vol.105 , pp. 593-600
    • Galvez, S.1    Bismuth, E.2    Sarda, C.3    Gadal, P.4
  • 16
    • 0027132883 scopus 로고
    • On the function of mitochondrial metabolism during photosynthesis in spinach (Spinacia oleracea L.) leaves
    • Hanning I, Heldt HW (1993) On the function of mitochondrial metabolism during photosynthesis in spinach (Spinacia oleracea L.) leaves. Plant Physiol 103: 1147-1154
    • (1993) Plant Physiol , vol.103 , pp. 1147-1154
    • Hanning, I.1    Heldt, H.W.2
  • 17
    • 0031949158 scopus 로고    scopus 로고
    • Antisense inhibition of cytosolic NADP-dependent isocitrate dehydrogenase in transgenic potato plants
    • Kruse A, Fieuw S, Heineke D, Muller-Rober B (1998) Antisense inhibition of cytosolic NADP-dependent isocitrate dehydrogenase in transgenic potato plants. Planta 205: 82-91
    • (1998) Planta , vol.205 , pp. 82-91
    • Kruse, A.1    Fieuw, S.2    Heineke, D.3    Muller-Rober, B.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of the structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of the structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0016313599 scopus 로고
    • Alternative route for nitrogen assimilation in higher plants
    • Lea PJ, Miflin BJ (1974) Alternative route for nitrogen assimilation in higher plants. Nature 251: 614-616
    • (1974) Nature , vol.251 , pp. 614-616
    • Lea, P.J.1    Miflin, B.J.2
  • 20
    • 0002564432 scopus 로고
    • +-linked isocitrate dehydrogenase: Isolation, purification, and characterization of the protein from pea mitochondria
    • +-linked isocitrate dehydrogenase: isolation, purification, and characterization of the protein from pea mitochondria. Plant Physiol 100: 69-75
    • (1992) Plant Physiol , vol.100 , pp. 69-75
    • McIntosh, C.A.1    Oliver, D.J.2
  • 21
    • 0002107129 scopus 로고
    • Ammonia assimilation and amino acid metabolism
    • D Boulter, B Parthier (eds) N S, Springer, New York
    • Miflin BJ, Lea PJ (1982) Ammonia assimilation and amino acid metabolism. In: D Boulter, B Parthier (eds) Encyclopedia of plant physiology, N S, vol 14 A. Springer, New York, pp 5-64
    • (1982) Encyclopedia of Plant Physiology , vol.14 A , pp. 5-64
    • Miflin, B.J.1    Lea, P.J.2
  • 23
    • 0027025560 scopus 로고
    • Molecular characterization and expression of an isocitrate dehydrogenase from alfalfa (Medicago sativa L.)
    • Shorrosh BS, Dixon RA (1992) Molecular characterization and expression of an isocitrate dehydrogenase from alfalfa (Medicago sativa L.). Plant Mol Biol 20: 801-807
    • (1992) Plant Mol Biol , vol.20 , pp. 801-807
    • Shorrosh, B.S.1    Dixon, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.