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Volumn 236, Issue 2, 1996, Pages 662-669

Cloning of Arabidopsis thaliana glutathione synthetase (GSH2) by functional complementation of a yeast gsh2 mutant

Author keywords

Arabidopsis thaliana; cadmium; evolutionary relationships; expression cloning; glutathione synthetase

Indexed keywords

GLUTATHIONE SYNTHASE;

EID: 0029965703     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00662.x     Document Type: Article
Times cited : (38)

References (60)
  • 1
    • 0029138945 scopus 로고
    • Dissection of oxidative stress tolerance using transgenic plants
    • Allen, R. D. (1995) Dissection of oxidative stress tolerance using transgenic plants, Plant Physiol. 107, 1049-1054.
    • (1995) Plant Physiol. , vol.107 , pp. 1049-1054
    • Allen, R.D.1
  • 2
    • 77956133444 scopus 로고
    • Biosynthesis and antioxidant function of glutathione in plants
    • Alscher, R. G. (1989) Biosynthesis and antioxidant function of glutathione in plants, Physiol. Plant. 77, 457-464.
    • (1989) Physiol. Plant. , vol.77 , pp. 457-464
    • Alscher, R.G.1
  • 4
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeast by electroporation
    • Becker, D. M. & Guarente, L. (1991) High-efficiency transformation of yeast by electroporation, Methods Enzymol. 194, 182-187.
    • (1991) Methods Enzymol. , vol.194 , pp. 182-187
    • Becker, D.M.1    Guarente, L.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0023887868 scopus 로고
    • Synthesis of functional mouse cytochromes P-450 P1 and chimeric P-450 P3-1 in the yeast Saccharomyces cerevisiae
    • Cullin, C. & Pompon, D. (1988) Synthesis of functional mouse cytochromes P-450 P1 and chimeric P-450 P3-1 in the yeast Saccharomyces cerevisiae, Gene (Amst.) 65, 203-217.
    • (1988) Gene (Amst.) , vol.65 , pp. 203-217
    • Cullin, C.1    Pompon, D.2
  • 7
    • 84983727785 scopus 로고
    • Effects of frost-hardening and salinity on glulathione and sulfhydryl levels and on glutathione reductase activity in spinach leaves
    • De Kok, L. J. & Oosterhuis, F. A. (1983) Effects of frost-hardening and salinity on glulathione and sulfhydryl levels and on glutathione reductase activity in spinach leaves, Physiol. Plant 58, 47-51.
    • (1983) Physiol. Plant , vol.58 , pp. 47-51
    • De Kok, L.J.1    Oosterhuis, F.A.2
  • 9
    • 0028111692 scopus 로고
    • Inhibition of tumour glyoxalase I by substituted glutathiones and hydroxy-quinone (and analogous) compounds
    • Douglas, K. T. & Keyworth, L. T. A. (1994) Inhibition of tumour glyoxalase I by substituted glutathiones and hydroxy-quinone (and analogous) compounds, Med. Sci. Res. 22, 641-642.
    • (1994) Med. Sci. Res. , vol.22 , pp. 641-642
    • Douglas, K.T.1    Keyworth, L.T.A.2
  • 11
    • 0025983098 scopus 로고
    • Evolution of glutathione metabolism
    • (Meister, A., ed.) Wiley Interscience
    • Fahey, R. C. & Sundquist, A. R. (1991) Evolution of glutathione metabolism, in Advances Enzymol. (Meister, A., ed.) vol. 64, pp. 1-53, Wiley Interscience.
    • (1991) Advances Enzymol. , vol.64 , pp. 1-53
    • Fahey, R.C.1    Sundquist, A.R.2
  • 12
    • 0028860295 scopus 로고
    • A common fold for peptide synthetases cleaving ATP to ADP: Glutathione synthetase and D-alanine:D-alanine ligase of Escherichia coli
    • Fan, C., Moews, P. C., Shi, Y., Walsh, C. T. & Knox, J. R. (1995) A common fold for peptide synthetases cleaving ATP to ADP: glutathione synthetase and D-alanine:D-alanine ligase of Escherichia coli, Proc. Natl Acad. Sci. USA 92, 1172-1176.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 1172-1176
    • Fan, C.1    Moews, P.C.2    Shi, Y.3    Walsh, C.T.4    Knox, J.R.5
  • 13
    • 0028010294 scopus 로고
    • Herbicide safeners and glutathione metabolism
    • Farago, S., Brunold, C. & Kreuz, K. (1994) Herbicide safeners and glutathione metabolism, Physiol. Plant. 91, 537-542.
    • (1994) Physiol. Plant. , vol.91 , pp. 537-542
    • Farago, S.1    Brunold, C.2    Kreuz, K.3
  • 14
    • 0000010851 scopus 로고
    • Responses of photosynthesis and the xanthophyll and ascorbate-glutathione cycles to changes in irradiance, photoinhibition and recovery
    • Foyer, C. H., Dujurdyn, M. & Lemoine, Y. (1989) Responses of photosynthesis and the xanthophyll and ascorbate-glutathione cycles to changes in irradiance, photoinhibition and recovery, Plant Physiol. Biochem. 27, 751-760.
    • (1989) Plant Physiol. Biochem. , vol.27 , pp. 751-760
    • Foyer, C.H.1    Dujurdyn, M.2    Lemoine, Y.3
  • 15
    • 0028129854 scopus 로고
    • A herbicide antidote (safener) induces the activity of both the herbicide detoxifying enzyme and of a vacuolar transporter for the detoxified herbicide
    • Gaillard, C., Dufaud, A., Tommasini, R., Kreuz, K., Amrhein, N. & Martinoia, E. (1994) A herbicide antidote (safener) induces the activity of both the herbicide detoxifying enzyme and of a vacuolar transporter for the detoxified herbicide, FEBS Lett. 352, 219-221.
    • (1994) FEBS Lett. , vol.352 , pp. 219-221
    • Gaillard, C.1    Dufaud, A.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5    Martinoia, E.6
  • 16
    • 0022379109 scopus 로고
    • Phytochelatins: The principal heavy-metal-binding peptides of higher plants
    • Grill, E., Winnacker, E. L. & Zenk, M. H. (1985) Phytochelatins: the principal heavy-metal-binding peptides of higher plants, Science 230, 674-676.
    • (1985) Science , vol.230 , pp. 674-676
    • Grill, E.1    Winnacker, E.L.2    Zenk, M.H.3
  • 17
    • 0001068301 scopus 로고
    • Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase)
    • Grill, E., Löffler, S., Winnacker, E.-L. & Zenk, M. H. (1989) Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific γ-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase), Proc. Natl Acad. Sci. USA 86, 6838-6842.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 6838-6842
    • Grill, E.1    Löffler, S.2    Winnacker, E.-L.3    Zenk, M.H.4
  • 18
    • 0021768603 scopus 로고
    • Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II
    • Gushima, H., Yasuda, S., Soeda, E., Yokota, M., Kondo, M. & Kimura, A. (1984) Complete nucleotide sequence of the E. coli glutathione synthetase gsh-II, Nucleic Acids Res. 12, 9299-9307.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 9299-9307
    • Gushima, H.1    Yasuda, S.2    Soeda, E.3    Yokota, M.4    Kondo, M.5    Kimura, A.6
  • 19
    • 0027185645 scopus 로고
    • Molecular cloning of the large subunit of glutathione synthetase from Xenopus laevis embryos
    • Habenicht, A., Hille, S. & Knöchel, W. (1993) Molecular cloning of the large subunit of glutathione synthetase from Xenopus laevis embryos, Biochim. Biophys. Acta 1174, 295-298.
    • (1993) Biochim. Biophys. Acta , vol.1174 , pp. 295-298
    • Habenicht, A.1    Hille, S.2    Knöchel, W.3
  • 21
    • 0001961690 scopus 로고
    • Glutathione synthetase in tobacco suspension cultures: Catalytic properties and localization
    • Hell, R. & Bergmann, L. (1988) Glutathione synthetase in tobacco suspension cultures: catalytic properties and localization, Physiol. Plant. 72, 70-76.
    • (1988) Physiol. Plant. , vol.72 , pp. 70-76
    • Hell, R.1    Bergmann, L.2
  • 22
    • 0028151944 scopus 로고
    • Influence of glutathione (GSH) on net uptake of sulfate and sulfate transport in tobacco plants
    • Herschbach, C. & Rennenberg, H. (1994) Influence of glutathione (GSH) on net uptake of sulfate and sulfate transport in tobacco plants, J. Exp. Bot. 45, 1069-1076.
    • (1994) J. Exp. Bot. , vol.45 , pp. 1069-1076
    • Herschbach, C.1    Rennenberg, H.2
  • 24
    • 0023481280 scopus 로고
    • A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli
    • Hoffman, C. S. & Winston, F. (1987) A ten-minute DNA preparation from yeast efficiently releases autonomous plasmids for transformation of Escherichia coli, Gene (Amst.) 57, 267-272.
    • (1987) Gene (Amst.) , vol.57 , pp. 267-272
    • Hoffman, C.S.1    Winston, F.2
  • 25
    • 0029278723 scopus 로고
    • A cadmium-sensitive, glulathione-deficient mutant of Arabidopsis thaliana
    • Howden, R., Andersen, C. R., Goldsbrough, P. B. & Cobbett, C. S. (1995) A cadmium-sensitive, glulathione-deficient mutant of Arabidopsis thaliana, Plant Physiol. 107, 1067-1073.
    • (1995) Plant Physiol. , vol.107 , pp. 1067-1073
    • Howden, R.1    Andersen, C.R.2    Goldsbrough, P.B.3    Cobbett, C.S.4
  • 27
    • 0023708260 scopus 로고
    • Role of cysteine residues in glutathione synthetase from Escherichia coli B
    • Kato, H., Tanaka, T., Nishioka, T., Kimura, A. & Oda, J. (1988) Role of cysteine residues in glutathione synthetase from Escherichia coli B, J. Biol. Chem. 263, 11 646-11 651.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11646-11651
    • Kato, H.1    Tanaka, T.2    Nishioka, T.3    Kimura, A.4    Oda, J.5
  • 28
    • 0022654951 scopus 로고
    • Isolation of glutathione-deficient mutants of the yeast Saccharomyces cerevisiae
    • Kistler, M., Summer, K.-H. & Eckardt, F. (1986) Isolation of glutathione-deficient mutants of the yeast Saccharomyces cerevisiae, Mutation Res. 173, 117-120.
    • (1986) Mutation Res. , vol.173 , pp. 117-120
    • Kistler, M.1    Summer, K.-H.2    Eckardt, F.3
  • 29
    • 1842411098 scopus 로고
    • Sulphur metabolism. E. Synthesis of glutathione
    • (Lea, P. J., ed.) Academic Press Inc., London
    • Klapheck, S. & Rennenberg, H. (1990) Sulphur metabolism. E. Synthesis of glutathione, in Methods in plant biochemistry (Lea, P. J., ed.) vol. 3, pp. 355-359, Academic Press Inc., London.
    • (1990) Methods in Plant Biochemistry , vol.3 , pp. 355-359
    • Klapheck, S.1    Rennenberg, H.2
  • 30
    • 84995019904 scopus 로고
    • γ-Glutamylcysteinylserine. A new homologue of glulathione in plants of the family poaceae
    • Klapheck, S., Chrost, B., Starke, J. & Zimmermann, H. (1992) γ-Glutamylcysteinylserine. A new homologue of glulathione in plants of the family poaceae, Bot. Acta 105, 174-179.
    • (1992) Bot. Acta , vol.105 , pp. 174-179
    • Klapheck, S.1    Chrost, B.2    Starke, J.3    Zimmermann, H.4
  • 31
    • 0026578156 scopus 로고
    • Saccharomyces cerevisiae and Neurospora crassa contain heavy metal sequestering phytochelatin
    • Kneer, R., Kutchan, T. M., Hochberger, A. & Zenk, M. H. (1992) Saccharomyces cerevisiae and Neurospora crassa contain heavy metal sequestering phytochelatin, Arch. Microbiol. 157, 305-310.
    • (1992) Arch. Microbiol. , vol.157 , pp. 305-310
    • Kneer, R.1    Kutchan, T.M.2    Hochberger, A.3    Zenk, M.H.4
  • 32
    • 0021196010 scopus 로고
    • Cadystin A and B, major unit peptides comprising cadmium binding peptides induced in a fission yeast separation, revision of structures and synthesis
    • Kondo, N., Imai, K., Iszobe, M., Goto, T., Murasugi, A., Wada-Nakawa, C. & Hayashi, Y. (1984) Cadystin A and B, major unit peptides comprising cadmium binding peptides induced in a fission yeast separation, revision of structures and synthesis, Tetrahedron Lett. 25, 3869-3872.
    • (1984) Tetrahedron Lett. , vol.25 , pp. 3869-3872
    • Kondo, N.1    Imai, K.2    Iszobe, M.3    Goto, T.4    Murasugi, A.5    Wada-Nakawa, C.6    Hayashi, Y.7
  • 33
    • 0023665902 scopus 로고
    • An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs
    • Kozak, M. (1987) An analysis of 5′-noncoding sequences from 699 vertebrate messenger RNAs, Nucleic Acids Res. 15, 8125-8133.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8125-8133
    • Kozak, M.1
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 38249043941 scopus 로고
    • Purification and properties of glutathione synthetase from spinach (Spinacia oleracea) leaves
    • Law, M. Y. & Halliwell, B. (1986) Purification and properties of glutathione synthetase from spinach (Spinacia oleracea) leaves, Plant Sci. 43, 185-191.
    • (1986) Plant Sci. , vol.43 , pp. 185-191
    • Law, M.Y.1    Halliwell, B.2
  • 36
    • 38249037265 scopus 로고
    • Homoglutathione and glutathione synthetases of legume seedlings: Partial purification and substrate specificity
    • Macnicol, P. K. (1987) Homoglutathione and glutathione synthetases of legume seedlings: partial purification and substrate specificity. Plant Sci. 53, 229-235.
    • (1987) Plant Sci. , vol.53 , pp. 229-235
    • Macnicol, P.K.1
  • 37
    • 0028170738 scopus 로고
    • Arabidopsis thaliana γ-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast, and Escherichia coli homologs
    • May, M. J. & Leaver, C. J. (1994) Arabidopsis thaliana γ-glutamylcysteine synthetase is structurally unrelated to mammalian, yeast, and Escherichia coli homologs, Proc. Natl Acad. Sci. USA 91, 10059-10063.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10059-10063
    • May, M.J.1    Leaver, C.J.2
  • 38
    • 77956912564 scopus 로고
    • Glulathione synthesis
    • (Boyer, P. D., ed.) 3rd edn, Academic Press Inc., New York
    • Meister, A. (1974) Glulathione synthesis, in The enzymes (Boyer, P. D., ed.) vol. 10, 3rd edn, pp. 671-697, Academic Press Inc., New York.
    • (1974) The Enzymes , vol.10 , pp. 671-697
    • Meister, A.1
  • 39
    • 0027787498 scopus 로고
    • γ-Glutamylcysteinylglutamic acid, a new homologue of glutathione in maize seedlings exposed to cadmium
    • Meuwly, P., Thibault, P. & Rauser, W. E. (1993) γ-Glutamylcysteinylglutamic acid, a new homologue of glutathione in maize seedlings exposed to cadmium, FEBS Lett. 336, 472-476.
    • (1993) FEBS Lett. , vol.336 , pp. 472-476
    • Meuwly, P.1    Thibault, P.2    Rauser, W.E.3
  • 40
    • 0026864596 scopus 로고
    • Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs
    • Minet, M., Dufour, M.-E. & Lacroute, F. (1992) Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs, Plant J. 2, 417-422.
    • (1992) Plant J. , vol.2 , pp. 417-422
    • Minet, M.1    Dufour, M.-E.2    Lacroute, F.3
  • 41
    • 0009267008 scopus 로고
    • Glutathione biosynthesis
    • Mooz, E. D. & Meister, A. (1971) Glutathione biosynthesis, Methods Enzymol. 17B, 483-495.
    • (1971) Methods Enzymol. , vol.17 B , pp. 483-495
    • Mooz, E.D.1    Meister, A.2
  • 42
    • 0028003648 scopus 로고
    • Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant detective in DNA synthesis
    • Muller, E. G. D. (1994) Deoxyribonucleotides are maintained at normal levels in a yeast thioredoxin mutant detective in DNA synthesis. J. Biol. Chem. 269, 24466-24471.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24466-24471
    • Muller, E.G.D.1
  • 43
    • 0024299219 scopus 로고
    • Isolation of mutants of Schizosaccharomyces pombe unable to synthesize cadystin, small cadmium-binding peptides
    • Mutoh, N. & Hayashi, Y. (1988) Isolation of mutants of Schizosaccharomyces pombe unable to synthesize cadystin, small cadmium-binding peptides, Biochem. Biophys. Res. Commun. 151, 32-39.
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 32-39
    • Mutoh, N.1    Hayashi, Y.2
  • 44
    • 0026326055 scopus 로고
    • Cloning and sequencing of the gene encoding the large subunit of glutathione synthetase of Schizosaccharomyces pombe
    • Mutoh, N., Nakagawa, C. W., Ando, S., Tanabe, K. & Hayashi, Y. (1991) Cloning and sequencing of the gene encoding the large subunit of glutathione synthetase of Schizosaccharomyces pombe, Biochem. Biophys. Res. Commun. 181, 430-436.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 430-436
    • Mutoh, N.1    Nakagawa, C.W.2    Ando, S.3    Tanabe, K.4    Hayashi, Y.5
  • 45
    • 0028949430 scopus 로고
    • Molecular cloning and nucleotide sequencing of the γ-glutamylcysteine synthetase gene of the fission yeast Schizosaccharomyces pombe
    • Mutoh, N., Nakagawa, C. W. & Hayashi, Y. (1995) Molecular cloning and nucleotide sequencing of the γ-glutamylcysteine synthetase gene of the fission yeast Schizosaccharomyces pombe, J. Biochem. 117, 283-288.
    • (1995) J. Biochem. , vol.117 , pp. 283-288
    • Mutoh, N.1    Nakagawa, C.W.2    Hayashi, Y.3
  • 46
    • 0001630848 scopus 로고
    • Isolation and characterization of glutathione biosynthesis-deficient mutants in Saccharomyces cerevisiae
    • Ohtake, Y., Satou, A. & Yabuuchi, S. (1990) Isolation and characterization of glutathione biosynthesis-deficient mutants in Saccharomyces cerevisiae, Agric. Biol. Chem. 54, 3145-3150.
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 3145-3150
    • Ohtake, Y.1    Satou, A.2    Yabuuchi, S.3
  • 47
    • 0026338492 scopus 로고
    • Molecular cloning of the γ-glutamylcysteine synthetase gene of Saccharomycex cerevisiae
    • Ohtake, Y. & Yabuuchi, S. (1991) Molecular cloning of the γ-glutamylcysteine synthetase gene of Saccharomycex cerevisiae, Yeast 7, 953-961.
    • (1991) Yeast , vol.7 , pp. 953-961
    • Ohtake, Y.1    Yabuuchi, S.2
  • 48
    • 0018801016 scopus 로고
    • Glutathione synthetase. Purification from rat kidney and mapping of the substrate binding sites
    • Oppenheimer, L., Wellner, V. P., Griffith, O. W. & Meister, A. (1979) Glutathione synthetase. Purification from rat kidney and mapping of the substrate binding sites, J. Biol. Chem. 254, 5184-5190.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5184-5190
    • Oppenheimer, L.1    Wellner, V.P.2    Griffith, O.W.3    Meister, A.4
  • 49
    • 0027412924 scopus 로고
    • Metabolism and functions of glutathione in micro-organisms
    • Penninckx, M. J. & Elskens, M. T. (1993) Metabolism and functions of glutathione in micro-organisms. Adv. Microb. Physiol. 34, 239-301.
    • (1993) Adv. Microb. Physiol. , vol.34 , pp. 239-301
    • Penninckx, M.J.1    Elskens, M.T.2
  • 50
    • 49149141770 scopus 로고
    • Glutathione metabolism and possible biological roles in higher plants
    • Rennenberg, H. (1982) Glutathione metabolism and possible biological roles in higher plants, Phytochemistry 21, 2771-2781.
    • (1982) Phytochemistry , vol.21 , pp. 2771-2781
    • Rennenberg, H.1
  • 52
    • 0000393627 scopus 로고
    • Localization of γ-glutamylcysteine synthetase and glutathione synthetase activity in maize seedlings
    • Rüegsegger, A. & Brunold, C. (1993) Localization of γ-glutamylcysteine synthetase and glutathione synthetase activity in maize seedlings, Plant. Physiol. 101, 561-566.
    • (1993) Plant. Physiol. , vol.101 , pp. 561-566
    • Rüegsegger, A.1    Brunold, C.2
  • 53
    • 0029140967 scopus 로고
    • Regulation of glutathione synthesis in suspension cultures of parsley and tobacco
    • Schneider, S. & Bergmann, L. (1995) Regulation of glutathione synthesis in suspension cultures of parsley and tobacco. Bot. Acta 108, 34-40.
    • (1995) Bot. Acta , vol.108 , pp. 34-40
    • Schneider, S.1    Bergmann, L.2
  • 54
    • 0026020420 scopus 로고
    • Vectors for expression of cloned genes in yeast: Regulation, overproduction, und underproduction
    • Schneider, J. C. & Guarente, L. (1991) Vectors for expression of cloned genes in yeast: regulation, overproduction, und underproduction, Methods Enzymol. 194, 373-388.
    • (1991) Methods Enzymol. , vol.194 , pp. 373-388
    • Schneider, J.C.1    Guarente, L.2
  • 55
    • 0029137960 scopus 로고
    • Regulation of glutathione synthesis in leaves of transgenic poplar (Populus tremula x P. alba) overexpressing glutathione synthetase
    • Strohm, M., Jouanin, L., Kunert, K. J., Pruvost, C., Polle, A., Foyer, C. H. & Rennenberg, H. (1995) Regulation of glutathione synthesis in leaves of transgenic poplar (Populus tremula x P. alba) overexpressing glutathione synthetase, Plant J. 7, 141-145.
    • (1995) Plant J. , vol.7 , pp. 141-145
    • Strohm, M.1    Jouanin, L.2    Kunert, K.J.3    Pruvost, C.4    Polle, A.5    Foyer, C.H.6    Rennenberg, H.7
  • 56
    • 0014481378 scopus 로고
    • Enzymic method for the quantitative determination of nanogram amounts of total and oxidized glutathione
    • Tietze, F. (1969) Enzymic method for the quantitative determination of nanogram amounts of total and oxidized glutathione, Anal. Biochem. 27, 502-522.
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 57
    • 0010528914 scopus 로고
    • Molecular characterization of corn glutathione S-transferase isozymes involved in herbicide detoxication
    • Timmerman, K. P. (1989) Molecular characterization of corn glutathione S-transferase isozymes involved in herbicide detoxication, Physiol. Plant. 77, 465-471.
    • (1989) Physiol. Plant. , vol.77 , pp. 465-471
    • Timmerman, K.P.1
  • 58
    • 0023046802 scopus 로고
    • The nucleotide sequence of the gene for γ-glutamylcysteine synthetase of Escherichia coli
    • Watanabe, K., Yamano, Y., Murata, K. & Kimura, A. (1986) The nucleotide sequence of the gene for γ-glutamylcysteine synthetase of Escherichia coli, Nucleic Acids Res. 14, 4393-4400.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4393-4400
    • Watanabe, K.1    Yamano, Y.2    Murata, K.3    Kimura, A.4
  • 59
    • 0027530140 scopus 로고
    • Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution
    • Yamaguchi, H., Kato, H., Hata, Y., Nishioka, T., Kimura, A., Oda, J. & Katsube, Y. (1993) Three-dimensional structure of the glutathione synthetase from Escherichia coli B at 2.0 Å resolution, J. Mol. Biol. 229, 1083-1100.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1083-1100
    • Yamaguchi, H.1    Kato, H.2    Hata, Y.3    Nishioka, T.4    Kimura, A.5    Oda, J.6    Katsube, Y.7
  • 60
    • 0025091990 scopus 로고
    • Amino acid sequence of rat kidney γ-glutamylcysteine synthetase
    • Yan, N. & Meister, A. (1990) Amino acid sequence of rat kidney γ-glutamylcysteine synthetase, J. Biol. Chem. 265, 1588-1593.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1588-1593
    • Yan, N.1    Meister, A.2


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