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Volumn 44, Issue 3, 1997, Pages 401-408

Biological role of oxaloacetate metabolism in chloroplasts of C3 plants

Author keywords

C3 plants; C4 dicarboxylic acids; Chloroplasts; Metabolism; Oxaloacetate decarboxylase

Indexed keywords


EID: 0031511044     PISSN: 10214437     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (79)
  • 2
    • 0004216109 scopus 로고
    • Translated under the title Moscow: Mir
    • Translated under the title Vvedenie v biokhimiyu rastenii, Moscow: Mir, 1986, vol. 1.
    • (1986) Vvedenie V Biokhimiyu Rastenii , vol.1
  • 3
    • 0004053615 scopus 로고
    • New York: Worth
    • Lehninger, A.L., Biochemistry, New York: Worth, 1972. Translated under the title Biokhimiya, Moscow: Mir, 1974.
    • (1972) Biochemistry
    • Lehninger, A.L.1
  • 4
    • 0039764823 scopus 로고
    • Translated under the title Moscow: Mir
    • Lehninger, A.L., Biochemistry, New York: Worth, 1972. Translated under the title Biokhimiya, Moscow: Mir, 1974.
    • (1974) Biokhimiya
  • 5
    • 0019316031 scopus 로고
    • Metabolic regulation by pH gradients: Inhibition of photosynthesis by indirect proton transfer across the chloroplast envelope
    • Enser, U. and Heber, U., Metabolic Regulation by pH Gradients: Inhibition of Photosynthesis by Indirect Proton Transfer across the Chloroplast Envelope, Biochim. Biophys. Acta, 1980, vol. 592, nos. 4-5, pp. 577-591.
    • (1980) Biochim. Biophys. Acta , vol.592 , Issue.4-5 , pp. 577-591
    • Enser, U.1    Heber, U.2
  • 6
    • 0011340184 scopus 로고
    • Pyruvate-derived amino acids in spinach chloroplasts: Synthesis and regulation during photosynthetic carbon metabolism
    • Schultze-Siebert, D., Heineke, D., Scharf, H., and Schultz, G., Pyruvate-derived Amino Acids in Spinach Chloroplasts: Synthesis and Regulation during Photosynthetic Carbon Metabolism, Plant Physiol., 1984, vol. 76, no. 2, pp. 465-471.
    • (1984) Plant Physiol. , vol.76 , Issue.2 , pp. 465-471
    • Schultze-Siebert, D.1    Heineke, D.2    Scharf, H.3    Schultz, G.4
  • 7
    • 0000357682 scopus 로고
    • Localization of pyruvate dehydrogenase complex in Pisum sativum chloroplasts
    • Elias, B.A. and Givan, C.V., Localization of Pyruvate Dehydrogenase Complex in Pisum sativum Chloroplasts, Plant Sci. Lett., 1979, vol. 17, no. 1, pp. 115-122.
    • (1979) Plant Sci. Lett. , vol.17 , Issue.1 , pp. 115-122
    • Elias, B.A.1    Givan, C.V.2
  • 8
    • 0001184797 scopus 로고
    • Pyruvate dehydrogenase complex from chloroplasts of Pisum sativum L
    • Williamce, M. and Randall, D.D., Pyruvate Dehydrogenase Complex from Chloroplasts of Pisum sativum L., Plant Physiol., 1979, vol. 64, no. 10, pp. 1099-1103.
    • (1979) Plant Physiol. , vol.64 , Issue.10 , pp. 1099-1103
    • Williamce, M.1    Randall, D.D.2
  • 9
    • 0001028416 scopus 로고
    • Purification and characterization of the pea chloroplast pyruvate dehydrogenase complex
    • Camp, P.J. and Randall, D.D., Purification and Characterization of the Pea Chloroplast Pyruvate Dehydrogenase Complex, Plant Physiol., 1985, vol. 77, no. 3, pp. 571-577.
    • (1985) Plant Physiol. , vol.77 , Issue.3 , pp. 571-577
    • Camp, P.J.1    Randall, D.D.2
  • 10
    • 0001158320 scopus 로고
    • Some kinetic and regulatory properties of the pea chloroplast dehydrogenase complex
    • Camp, P.J., Miernyk, J.A., and Randall, D.D., Some Kinetic and Regulatory Properties of the Pea Chloroplast Dehydrogenase Complex, Biochim. Biophys. Acta: Bioenergetics, 1988, vol. 933, no. 2, pp. 269-275.
    • (1988) Biochim. Biophys. Acta: Bioenergetics , vol.933 , Issue.2 , pp. 269-275
    • Camp, P.J.1    Miernyk, J.A.2    Randall, D.D.3
  • 11
    • 0018602747 scopus 로고
    • Acetate is the preferred substrate for long-chain fatty acid synthesis in isolated spinach chloroplasts
    • Roughan, H.G., Holland, R., and Slack, C.R., Acetate Is the Preferred Substrate for Long-Chain Fatty Acid Synthesis in Isolated Spinach Chloroplasts, Biochem. J., 1979, vol. 184, no. 3, pp. 565-569.
    • (1979) Biochem. J. , vol.184 , Issue.3 , pp. 565-569
    • Roughan, H.G.1    Holland, R.2    Slack, C.R.3
  • 12
    • 0002026724 scopus 로고
    • A specific translocator for oxaloacetate transport in chloroplasts
    • Hatch, M.D., Dröscher, L., Flügge, U.I., and Heldt, H.W., A Specific Translocator for Oxaloacetate Transport in Chloroplasts, FEBS Lett., 1984, vol. 178, no. 1, pp. 15-19.
    • (1984) FEBS Lett. , vol.178 , Issue.1 , pp. 15-19
    • Hatch, M.D.1    Dröscher, L.2    Flügge, U.I.3    Heldt, H.W.4
  • 14
    • 0039038628 scopus 로고
    • 3-plant leaves
    • 3-Plant Leaves, Fiziol. Rast. (Moscow), 1990, vol. 37, no. 6, pp. 1065-1071 (Sov. Plant Physiol., Engl. Transl.).
    • (1990) Fiziol. Rast. (Moscow) , vol.37 , Issue.6 , pp. 1065-1071
    • Ivanishchev, V.V.1
  • 15
    • 85017245571 scopus 로고    scopus 로고
    • Engl. Transl.
    • 3-Plant Leaves, Fiziol. Rast. (Moscow), 1990, vol. 37, no. 6, pp. 1065-1071 (Sov. Plant Physiol., Engl. Transl.).
    • Sov. Plant Physiol.
  • 16
    • 0014150029 scopus 로고
    • Oxaloacetate decarboxylase of Aerobacter aerogenes. I. Inhibition by avidin and requirement for sodium ion
    • Stern, J.R., Oxaloacetate Decarboxylase of Aerobacter aerogenes. I. Inhibition by Avidin and Requirement for Sodium Ion, Biochemistry, 1967, vol. 6, no. 11, pp. 3545-3551.
    • (1967) Biochemistry , vol.6 , Issue.11 , pp. 3545-3551
    • Stern, J.R.1
  • 17
    • 0014368091 scopus 로고
    • Oxaloacetate decarboxylase from cod: A shorter preparation and crystallization
    • Kosicki, G.W., Oxaloacetate Decarboxylase from Cod: A Shorter Preparation and Crystallization, Biochemistry, 1968, vol. 7, no. 12, pp. 4299-4302.
    • (1968) Biochemistry , vol.7 , Issue.12 , pp. 4299-4302
    • Kosicki, G.W.1
  • 18
    • 0019475514 scopus 로고
    • Characterization of a membrane-bound biotin-containing enzyme: Oxaloacetate decarboxylase from Klebsiella aerogenes
    • Dimroth, P., Characterization of a Membrane-bound Biotin-containing Enzyme: Oxaloacetate Decarboxylase from Klebsiella aerogenes, Eur. J. Biochem., 1981, vol. 115, no. 2, pp. 353-358.
    • (1981) Eur. J. Biochem. , vol.115 , Issue.2 , pp. 353-358
    • Dimroth, P.1
  • 19
    • 0039038626 scopus 로고
    • Effect of substrate on oxaloacetate decarboxylase activity of cotton leaf chloroplasts
    • Ivanishchev, V.V., Effect of Substrate on Oxaloacetate Decarboxylase Activity of Cotton Leaf Chloroplasts, Dokl. Akad. Nauk Tadzh. SSR, 1989, vol. 32, no. 3, pp. 202-205.
    • (1989) Dokl. Akad. Nauk Tadzh. SSR , vol.32 , Issue.3 , pp. 202-205
    • Ivanishchev, V.V.1
  • 20
    • 0003355284 scopus 로고
    • Glyoxysomal and mitochondrial malate dehydrogenase of watermelon (Citrullus vulgaris) cotyledons: II. Kinetic properties of the purified isoenzymes
    • Walk, R.A. and Hock, B., Glyoxysomal and Mitochondrial Malate Dehydrogenase of Watermelon (Citrullus vulgaris) Cotyledons: II. Kinetic Properties of the Purified Isoenzymes, Planta, 1977, vol. 136, no. 3, pp. 221-228.
    • (1977) Planta , vol.136 , Issue.3 , pp. 221-228
    • Walk, R.A.1    Hock, B.2
  • 21
    • 0039038560 scopus 로고
    • Effect of pH on oxaloaceatate-decarboxylase activity of cotton leaf chloroplasts
    • Ivanishchev, V. V., Effect of pH on Oxaloaceatate-Decarboxylase Activity of Cotton Leaf Chloroplasts, Dokl. Akad. Nauk Tadzh. SSR, 1989, vol. 32, no. 4, pp. 77-279.
    • (1989) Dokl. Akad. Nauk Tadzh. SSR , vol.32 , Issue.4 , pp. 77-279
    • Ivanishchev, V.V.1
  • 22
    • 0020993273 scopus 로고
    • Subunit composition of oxaloacetate decarboxylase and characterization of the α-chain as carboxyltransferase
    • Dimroth, P. and Thomer, A., Subunit Composition of Oxaloacetate Decarboxylase and Characterization of the α-Chain as Carboxyltransferase, Eur. J. Biochem., 1983, vol. 137, no. 1, pp. 107-112.
    • (1983) Eur. J. Biochem. , vol.137 , Issue.1 , pp. 107-112
    • Dimroth, P.1    Thomer, A.2
  • 23
    • 0023692314 scopus 로고
    • Oxaloacetate decarboxylase from Klebsiella pneumoniae: Size and shape of the enzyme, and localization of its prostetic biotine group by electron microscopic affinity labelling
    • Dakena, P., Ronde, M., Dimroth, P., and Mayer, F., Oxaloacetate Decarboxylase from Klebsiella pneumoniae: Size and Shape of the Enzyme, and Localization of Its Prostetic Biotine Group by Electron Microscopic Affinity Labelling, FEMS Microbiol. Lett., 1988, vol. 55, no. 1, pp. 35-40.
    • (1988) FEMS Microbiol. Lett. , vol.55 , Issue.1 , pp. 35-40
    • Dakena, P.1    Ronde, M.2    Dimroth, P.3    Mayer, F.4
  • 24
    • 0039630646 scopus 로고
    • Isolation of highly-purified oxaloacetate decarboxylase from sunflower chloroplasts and some of its properties
    • Ivanishchev, V.V., Isolation of Highly-purified Oxaloacetate Decarboxylase from Sunflower Chloroplasts and Some of Its Properties, Fisiol. Rast. (Moscow), 1992, vol. 39, no. 4, pp. 760-768 (Sov. Plant Physiol., Engl. Transl.).
    • (1992) Fisiol. Rast. (Moscow) , vol.39 , Issue.4 , pp. 760-768
    • Ivanishchev, V.V.1
  • 25
    • 85017245571 scopus 로고    scopus 로고
    • Engl. Transl.
    • Ivanishchev, V.V., Isolation of Highly-purified Oxaloacetate Decarboxylase from Sunflower Chloroplasts and Some of Its Properties, Fisiol. Rast. (Moscow), 1992, vol. 39, no. 4, pp. 760-768 (Sov. Plant Physiol., Engl. Transl.).
    • Sov. Plant Physiol.
  • 26
    • 0018472736 scopus 로고
    • NADP-Malic enzyme from maize leaf: Purification, and properties
    • Asami, S., Inoue, K., Matsumoto, K., Murachi, A., and Akazawa, T., NADP-Malic Enzyme from Maize Leaf: Purification, and Properties, Arch. Biochem. Biophys., 1979, vol. 194, no. 2, pp. 503-510.
    • (1979) Arch. Biochem. Biophys. , vol.194 , Issue.2 , pp. 503-510
    • Asami, S.1    Inoue, K.2    Matsumoto, K.3    Murachi, A.4    Akazawa, T.5
  • 27
    • 0018293075 scopus 로고
    • 2+ serves as divalent cation
    • 2+ Serves as Divalent Cation, Biochemistry, 1979, vol. 18, no. 16, pp. 3604-3610.
    • (1979) Biochemistry , vol.18 , Issue.16 , pp. 3604-3610
    • Milne, J.A.1    Cook, R.A.2
  • 28
    • 0022742485 scopus 로고
    • pH-Dependence of kinetic parameters for oxaloacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme
    • Park, S.-H., Harris, B.G., and Cook, P.F., pH-Dependence of Kinetic Parameters for Oxaloacetate Decarboxylation and Pyruvate Reduction Reactions Catalyzed by Malic Enzyme, Biochemistry, 1986, vol. 25, no. 13, pp. 3752-3759.
    • (1986) Biochemistry , vol.25 , Issue.13 , pp. 3752-3759
    • Park, S.-H.1    Harris, B.G.2    Cook, P.F.3
  • 29
    • 0039038624 scopus 로고
    • Malate dehydrogenase isoenzymes from cotton leaves
    • O'Sullivan, S.A. and Wedding, R.T., Malate Dehydrogenase Isoenzymes from Cotton Leaves, Plant Physiol., 1972, vol. 49, no. 2, pp. 117-123.
    • (1972) Plant Physiol. , vol.49 , Issue.2 , pp. 117-123
    • O'Sullivan, S.A.1    Wedding, R.T.2
  • 30
    • 0022447351 scopus 로고
    • Kinetic analysis of the reaction mechanism of oxaloacetate decarboxylase from Klebsiella aerogenes
    • Dimroth, P. and Thomer, A., Kinetic Analysis of the Reaction Mechanism of Oxaloacetate Decarboxylase from Klebsiella aerogenes, Eur. J. Biochem., 1986, vol. 156, no. 1, pp. 157-162.
    • (1986) Eur. J. Biochem. , vol.156 , Issue.1 , pp. 157-162
    • Dimroth, P.1    Thomer, A.2
  • 31
    • 0039038627 scopus 로고
    • On properties of oxaloacetate decarboxylase from sunflower chloroplasts
    • Ivanishchev, V.V., On Properties of Oxaloacetate Decarboxylase from Sunflower Chloroplasts, Dokl. Akad. Nauk Tadzh. SSR, 1990, vol. 33, no. 11, pp. 774-777.
    • (1990) Dokl. Akad. Nauk Tadzh. SSR , vol.33 , Issue.11 , pp. 774-777
    • Ivanishchev, V.V.1
  • 32
    • 0039630649 scopus 로고
    • Properties of oxaloacetate decarboxylase from sunflower leaf chloroplasts
    • Ivanishchev, V.V. and Kurganov, B.I., Properties of Oxaloacetate Decarboxylase from Sunflower Leaf Chloroplasts, Biokhimiya (Moscow), 1993, vol. 58, no. 2, pp. 250-254.
    • (1993) Biokhimiya (Moscow) , vol.58 , Issue.2 , pp. 250-254
    • Ivanishchev, V.V.1    Kurganov, B.I.2
  • 33
    • 0017581550 scopus 로고
    • Novel enzymic machinery for the metabolism of oxaloacetate, phosphoenolpyruvate, and pyruvate in Pseudomonas citronellolis
    • O'Brien, R.W, Chuang, D.T., Taylor, B.L., and Utter, M.F., Novel Enzymic Machinery for the Metabolism of Oxaloacetate, Phosphoenolpyruvate, and Pyruvate in Pseudomonas citronellolis, J. Biol. Chem., 1977, vol. 252, no. 4, pp. 1257-1263.
    • (1977) J. Biol. Chem. , vol.252 , Issue.4 , pp. 1257-1263
    • O'Brien, R.W.1    Chuang, D.T.2    Taylor, B.L.3    Utter, M.F.4
  • 34
    • 0039038625 scopus 로고
    • Regulation of adenylate levels in intact spinach chloroplasts
    • Kobayashi, Y., Inoue, Y., Furuya, E, Shibata, K., and Heber, U., Regulation of Adenylate Levels in Intact Spinach Chloroplasts, Planta, 1979, vol. 147, no. 1, pp. 68-75.
    • (1979) Planta , vol.147 , Issue.1 , pp. 68-75
    • Kobayashi, Y.1    Inoue, Y.2    Furuya, E.3    Shibata, K.4    Heber, U.5
  • 35
    • 0040817160 scopus 로고
    • Alteration in the activity of chloroplast enzymes converting oxaloacetate in the course of plant growth and development
    • Ivanishchev, V.V., Alteration in the Activity of Chloroplast Enzymes Converting Oxaloacetate in the Course of Plant Growth and Development, Dokl. Akad. Nauk Resp. Tadzh., 1992, vol. 35, nos. 3-4, pp. 211-215.
    • (1992) Dokl. Akad. Nauk Resp. Tadzh. , vol.35 , Issue.3-4 , pp. 211-215
    • Ivanishchev, V.V.1
  • 36
    • 0040222587 scopus 로고
    • Molecular and kinetic properties and the regulation of activity in the enzymes metabolizing oxaloacetate in plant cell
    • Dushanbe: Institute of Plant Physiology and Biophysics
    • Ivanishchev, V.V., Molecular and Kinetic Properties and the Regulation of Activity in the Enzymes Metabolizing Oxaloacetate in Plant Cell, Doctoral (Biol.) Dissertation, Dushanbe: Institute of Plant Physiology and Biophysics, 1992.
    • (1992) Doctoral (Biol.) Dissertation
    • Ivanishchev, V.V.1
  • 38
    • 0000995253 scopus 로고
    • 2 assimilation and carbon flux in the calvin cycle and the glycolate pathway in water-stressed sunflower and bean leaves
    • 2 Assimilation and Carbon Flux in the Calvin Cycle and the Glycolate Pathway in Water-stressed Sunflower and Bean Leaves, Photosynthetica, 1984, vol. 18, no. 3, pp. 329-337.
    • (1984) Photosynthetica , vol.18 , Issue.3 , pp. 329-337
    • Krampitz, M.J.1    Fock, H.P.2
  • 39
    • 0039630640 scopus 로고
    • Effect of chloride and sulphate type of salinity on some metabolic drifts in chickpea, Cicer arietinum
    • Sharma, K.D., Datta, K.S., and Varma, S.K., Effect of Chloride and Sulphate Type of Salinity on Some Metabolic Drifts in Chickpea, Cicer arietinum, Ind. J. Exp. Biol., 1990, vol. 28, no. 9, pp. 890-892.
    • (1990) Ind. J. Exp. Biol. , vol.28 , Issue.9 , pp. 890-892
    • Sharma, K.D.1    Datta, K.S.2    Varma, S.K.3
  • 41
    • 85017245571 scopus 로고    scopus 로고
    • Engl. Transl.
    • 4-Acid Metabolism in Rye Chloroplasts, Fiziol. Rast. (Moscow), 1989, vol. 36, no. 4, pp. 665-668 (Sov. Plant Physiol., Engl. Transl.).
    • Sov. Plant Physiol.
  • 42
    • 1842406140 scopus 로고
    • Partitioning of malate dehydrogenase isoenzymes into glyoxysomes, mitochondria, and chloroplasts
    • Gietl, C., Partitioning of Malate Dehydrogenase Isoenzymes into Glyoxysomes, Mitochondria, and Chloroplasts, Plant Physiol., 1992, vol. 100, no. 2, pp. 557-559.
    • (1992) Plant Physiol. , vol.100 , Issue.2 , pp. 557-559
    • Gietl, C.1
  • 43
    • 38249031512 scopus 로고
    • The intracellular localization of malate dehydrogenase in Anacystis nidulans
    • Sallal, A.-K. J. and Nimer, N.A., The Intracellular Localization of Malate Dehydrogenase in Anacystis nidulans, FEMS Microbiol. Lett., 1988, vol. 50, nos. 2-3, pp. 151-155.
    • (1988) FEMS Microbiol. Lett. , vol.50 , Issue.2-3 , pp. 151-155
    • Sallal, A.-K.J.1    Nimer, N.A.2
  • 44
    • 0000330794 scopus 로고
    • Carboanhydrase activity in chloroplasts and chloroplast fragments
    • Vaklinova, S.G., Goushtiona, L.M., and Lazova, G.N., Carboanhydrase Activity in Chloroplasts and Chloroplast Fragments, C. R. Bulg. Acad. Sci., 1982, vol. 35, no. 12, pp. 1721-1724.
    • (1982) C. R. Bulg. Acad. Sci. , vol.35 , Issue.12 , pp. 1721-1724
    • Vaklinova, S.G.1    Goushtiona, L.M.2    Lazova, G.N.3
  • 45
    • 0040817159 scopus 로고
    • Towards a model for malate accumulation in plant tissues
    • Ting, I.P., Towards a Model for Malate Accumulation in Plant Tissues, Plant Sci. Lett., 1981, vol. 21, no. 2, pp. 215-221.
    • (1981) Plant Sci. Lett. , vol.21 , Issue.2 , pp. 215-221
    • Ting, I.P.1
  • 46
    • 0019084880 scopus 로고
    • Intracellular metabolite gradients and flow of carbon during photosynthesis of leaf protoplasts
    • Giersch, C., Heber, H., Kaiser, G., Walker, D.A., and Robinson, S.P., Intracellular Metabolite Gradients and Flow of Carbon during Photosynthesis of Leaf Protoplasts, Arch. Biochem. Biophys., 1980, vol. 205, no. 2, pp. 246-259.
    • (1980) Arch. Biochem. Biophys. , vol.205 , Issue.2 , pp. 246-259
    • Giersch, C.1    Heber, H.2    Kaiser, G.3    Walker, D.A.4    Robinson, S.P.5
  • 47
    • 0001411962 scopus 로고
    • Metabolite exchange between chloroplasts and cytoplasm
    • Heber, U., Metabolite Exchange between Chloroplasts and Cytoplasm, Annu. Rev. Plant Physiol., 1974, vol. 25, pp. 393-421.
    • (1974) Annu. Rev. Plant Physiol. , vol.25 , pp. 393-421
    • Heber, U.1
  • 48
    • 0013855646 scopus 로고
    • Compartmentation and reduction of pyridine nucleotides in relation to photosynthesis
    • Heber, U.W. and Santarius, K.A., Compartmentation and Reduction of Pyridine Nucleotides in Relation to Photosynthesis, Biochim. Biophys. Acta, 1965, vol. 109, no. 2, pp. 390-408.
    • (1965) Biochim. Biophys. Acta , vol.109 , Issue.2 , pp. 390-408
    • Heber, U.W.1    Santarius, K.A.2
  • 49
    • 0000441567 scopus 로고
    • NADP regulates the light activation of NADP-dependent malate dehydrogenase
    • Scheibe, R. and Jacquot, J.-P., NADP Regulates the Light Activation of NADP-Dependent Malate Dehydrogenase, Planta, 1983, vol. 157, no. 6, pp. 548-553.
    • (1983) Planta , vol.157 , Issue.6 , pp. 548-553
    • Scheibe, R.1    Jacquot, J.-P.2
  • 50
    • 38249035439 scopus 로고
    • Interaction between ribulose-1,5-bisphosphate carboxylase and stromal metabolites: II. Corraboration of the role of this enzyme as a metabolite buffer
    • Furbank, R.T., Foyer, C.H., and Walker, D.A., Interaction between Ribulose-1,5-Bisphosphate Carboxylase and Stromal Metabolites: II. Corraboration of the Role of this Enzyme as a Metabolite Buffer, Biochim. Biophys. Acta: Bioenergetics, 1987, vol. 894, no. 2, pp. 165-173.
    • (1987) Biochim. Biophys. Acta: Bioenergetics , vol.894 , Issue.2 , pp. 165-173
    • Furbank, R.T.1    Foyer, C.H.2    Walker, D.A.3
  • 51
    • 0018791242 scopus 로고
    • 2 incorporation into 4-carbon and 3-carbon intermediates
    • 2 Incorporation into 4-Carbon and 3-Carbon Intermediates, Arch. Biochem. Biophys., 1979, vol. 194, no. 4, pp. 117-127.
    • (1979) Arch. Biochem. Biophys. , vol.194 , Issue.4 , pp. 117-127
    • Hatch, M.D.1
  • 52
    • 0040817161 scopus 로고
    • 2-concentrating mechanism
    • 2-concentrating Mechanism, Fiziol. Rast. (Moscow), 1992, vol. 39, no. 3, pp. 437-444 (Sov. Plant Physiol., Engl. Transl.).
    • (1992) Fiziol. Rast. (Moscow) , vol.39 , Issue.3 , pp. 437-444
    • Ivanishchev, V.V.1
  • 53
    • 85017245571 scopus 로고    scopus 로고
    • Engl. Transl.
    • 2-concentrating Mechanism, Fiziol. Rast. (Moscow), 1992, vol. 39, no. 3, pp. 437-444 (Sov. Plant Physiol., Engl. Transl.).
    • Sov. Plant Physiol.
  • 55
    • 0018653244 scopus 로고
    • 2 biodynamics: A new type of cellular control
    • 2 Biodynamics: A New Type of Cellular Control, J. Theor. Biol., 1979, vol. 80, no. 3, pp. 537-551.
    • (1979) J. Theor. Biol. , vol.80 , Issue.3 , pp. 537-551
    • Mitz, M.A.1
  • 56
    • 0020066052 scopus 로고
    • Kinetic characteristics of bicarbonate-cloride exchange across the neonatal human red cell membrane
    • Chow, E.I. and Chen, D., Kinetic Characteristics of Bicarbonate-Cloride Exchange across the Neonatal Human Red Cell Membrane, Biochim. Biophys. Acta, 1982, vol. 685, no. 2, pp. 196-202.
    • (1982) Biochim. Biophys. Acta , vol.685 , Issue.2 , pp. 196-202
    • Chow, E.I.1    Chen, D.2
  • 57
    • 0021749661 scopus 로고
    • Carboxylation of pyruvate and acetyl coenzyme-A and methylmalonyl-CoA
    • Dimroth, P. and Hilpert, W., Carboxylation of Pyruvate and Acetyl Coenzyme-A and Methylmalonyl-CoA, Biochemistry, 1984, vol. 23, no. 22, pp. 5360-5366.
    • (1984) Biochemistry , vol.23 , Issue.22 , pp. 5360-5366
    • Dimroth, P.1    Hilpert, W.2
  • 58
    • 0024500243 scopus 로고
    • Bicarbonate and pH, response
    • Thomas, R.C., Bicarbonate and pH, Response, Nature, 1989, vol. 337, no. 6208, p. 601.
    • (1989) Nature , vol.337 , Issue.6208 , pp. 601
    • Thomas, R.C.1
  • 59
    • 0040222586 scopus 로고
    • Effect of exogenous carboanhydrase on photosynthetic electron transport and phosphorylation
    • Shin, I.V., Firus, O.K., Lazova, G.N., and Giller, Yu. E., Effect of Exogenous Carboanhydrase on Photosynthetic Electron Transport and Phosphorylation, Dokl. Akad. Nauk SSSR, 1989, vol. 304, no. 1, pp. 252-255.
    • (1989) Dokl. Akad. Nauk SSSR , vol.304 , Issue.1 , pp. 252-255
    • Shin, I.V.1    Firus, O.K.2    Lazova, G.N.3    Giller, Yu.E.4
  • 61
    • 85017245571 scopus 로고    scopus 로고
    • Engl. Transl.
    • 2 Concentration, Fiziol. Rast. (Moscow), 1981, vol. 28, no. 3, pp. 494-502 (Sov. Plant Physiol., Engl. Transl.).
    • Sov. Plant Physiol.
  • 62
    • 0039038621 scopus 로고
    • A proposed mechanism for the stimulatory effect of bicarbonate ions on ATP synthesis in isolated chloroplasts
    • Cohen, W.S. and Mac Peek, W.A., A Proposed Mechanism for the Stimulatory Effect of Bicarbonate Ions on ATP Synthesis in Isolated Chloroplasts, Plant Physiol., 1980, vol. 66, no. 2, pp. 242-245.
    • (1980) Plant Physiol. , vol.66 , Issue.2 , pp. 242-245
    • Cohen, W.S.1    Mac Peek, W.A.2
  • 63
    • 0000634951 scopus 로고
    • 2 concentration on protein biosynthesis and carbonic anhydrase expression in chlamydomonas reinhardtii
    • 2 Concentration on Protein Biosynthesis and Carbonic Anhydrase Expression in Chlamydomonas reinhardtii, Plant Physiol., 1988, vol. 87, no. 4, pp. 833-840.
    • (1988) Plant Physiol. , vol.87 , Issue.4 , pp. 833-840
    • Bailly, J.1    Coleman, J.R.2
  • 65
    • 0039050486 scopus 로고
    • Genetic regulation of development and activity of the photosynthetic apparatus
    • Nichiporovich, A.A., Ed., Moscow: Nauka
    • Nasyrov, Yu. S., Genetic Regulation of Development and Activity of the Photosynthetic Apparatus, Fiziologiya fotosinteza (Physiology of Photosynthesis), Nichiporovich, A.A., Ed., Moscow: Nauka, 1982, pp. 146-164.
    • (1982) Fiziologiya Fotosinteza (Physiology of Photosynthesis) , pp. 146-164
    • Nasyrov, Yu.S.1
  • 66
    • 0038170716 scopus 로고
    • 14C]phosphoglycerate by isolated intact spinach chloroplasts. Evidence for a chloroplastic 3-phosphoglycerate-2-phosphoglycerate-posphoenolpyruvate-pyruvate pathway
    • 14C]Phosphoglycerate by Isolated Intact Spinach Chloroplasts. Evidence for a Chloroplastic 3-Phosphoglycerate-2-Phosphoglycerate-Posphoenolpyruvate-Pyruvate Pathway, Plant Sci., 1989, vol. 59, no. 2, pp. 167-174.
    • (1989) Plant Sci. , vol.59 , Issue.2 , pp. 167-174
    • Schultze-Siebert, D.1    Schultz, G.2
  • 67
    • 0039038623 scopus 로고
    • 4-dicarboxylic acids by intact spinach chloroplasts
    • 4-Dicarboxylic Acids by Intact Spinach Chloroplasts, Planta, 1975, vol. 125, no. 1, pp. 63-67.
    • (1975) Planta , vol.125 , Issue.1 , pp. 63-67
    • Scheibe, R.1    Beck, E.2
  • 68
    • 0008688535 scopus 로고
    • Fatty acid synthesis by spinach chloroplasts: H. The path from PGA to fatty acids
    • Yamada, M. and Nakamura, Y., Fatty Acid Synthesis by Spinach Chloroplasts: H. The Path from PGA to Fatty Acids, Plant Cell Physiol., 1975, vol. 16, no. 1, pp. 151-162.
    • (1975) Plant Cell Physiol. , vol.16 , Issue.1 , pp. 151-162
    • Yamada, M.1    Nakamura, Y.2
  • 69
    • 0000242855 scopus 로고
    • Maintenance of high photosynthetic rates during the accumulation of high leaf starch levels in sunflower and soybean
    • Potter, J.R., Maintenance of High Photosynthetic Rates during the Accumulation of High Leaf Starch Levels in Sunflower and Soybean, Plant Physiol., 1980, vol. 66, no. 3, pp. 528-531.
    • (1980) Plant Physiol. , vol.66 , Issue.3 , pp. 528-531
    • Potter, J.R.1
  • 72
    • 0039630642 scopus 로고
    • Study of enzymes of phosphoenolpyruvate biosynthesis and oxaloacetate utilization in isogenic pea mutants
    • Ivanishchev, V.V. and Gorenkova, L.G., Study of Enzymes of Phosphoenolpyruvate Biosynthesis and Oxaloacetate Utilization in Isogenic Pea Mutants, Fiziol. Rast. (Moscow), 1995, vol. 42, no. 5, pp. 754-758 (Rus. J. Plant Physiol., Engl. Transl.).
    • (1995) Fiziol. Rast. (Moscow) , vol.42 , Issue.5 , pp. 754-758
    • Ivanishchev, V.V.1    Gorenkova, L.G.2
  • 73
    • 0040817163 scopus 로고    scopus 로고
    • Engl. Transl.
    • Ivanishchev, V.V. and Gorenkova, L.G., Study of Enzymes of Phosphoenolpyruvate Biosynthesis and Oxaloacetate Utilization in Isogenic Pea Mutants, Fiziol. Rast. (Moscow), 1995, vol. 42, no. 5, pp. 754-758 (Rus. J. Plant Physiol., Engl. Transl.).
    • Rus. J. Plant Physiol.
  • 74
    • 0040817162 scopus 로고    scopus 로고
    • US Patent 4757009 ICI C 12 P 13/04, C 12 N 15/00, Ajinomoto Co., Inc., N 645107, 1988
    • Sano, K., Ito, K., Miwa, K., and Nakamori, S., US Patent 4757009 ICI C 12 P 13/04, C 12 N 15/00, Ajinomoto Co., Inc., N 645107, 1988.
    • Sano, K.1    Ito, K.2    Miwa, K.3    Nakamori, S.4
  • 77
    • 84961475162 scopus 로고
    • Intracellular conversion of malate and localization of enzymes involved in the metabolism of malate in photoautotrophic cell cultures of Chenopodium rubrum
    • Amino Shin-ichi, Intracellular Conversion of Malate and Localization of Enzymes Involved in the Metabolism of Malate in Photoautotrophic Cell Cultures of Chenopodium rubrum, Z. Naturforsch. C: Biosci., 1992, vol. 47, nos. 7-8, pp. 545-552.
    • (1992) Z. Naturforsch. C: Biosci. , vol.47 , Issue.7-8 , pp. 545-552
    • Shin-Ichi, A.1
  • 78
    • 0001080443 scopus 로고
    • Malate and pyruvate-dependent fatty acid synthesis in leucoplasts from developing castor endosperm
    • Smith, R.G., Ganthier, D.A., Dennis, D.T., andTurpin, D.H., Malate and Pyruvate-Dependent Fatty Acid Synthesis in Leucoplasts from Developing Castor Endosperm, Plant Physiol., 1992, vol. 98, no. 4, pp. 1233-1238.
    • (1992) Plant Physiol. , vol.98 , Issue.4 , pp. 1233-1238
    • Smith, R.G.1    Ganthier, D.A.2    Dennis, D.T.3    Turpin, D.H.4
  • 79
    • 0040222584 scopus 로고
    • Polarographic study of dicarboxylic-acid-dependent export of reducing equivalents from illuminated chloroplasts
    • Anderson, J.W. and House, C.M., Polarographic Study of Dicarboxylic-Acid-Dependent Export of Reducing Equivalents from Illuminated Chloroplasts, Plant Physiol., 1979, vol. 64, no. 6, pp. 1064-1069.
    • (1979) Plant Physiol. , vol.64 , Issue.6 , pp. 1064-1069
    • Anderson, J.W.1    House, C.M.2


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