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Volumn 38, Issue 10, 1997, Pages 1150-1155

Purification and characterization of arginine decarboxylase from soybean (Glycine max) hypocotyls

Author keywords

Agmatine; Arginine decarboxylase (EC 4.1.1.19); Molecular weight; Polyamines; Soybean (Glycine max) hypocotyls

Indexed keywords

GLYCINE MAX;

EID: 0000984820     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.pcp.a029100     Document Type: Article
Times cited : (15)

References (28)
  • 1
    • 0021759133 scopus 로고
    • Purification and properties of ornithine decarboxylase from Physarum polycephalum
    • Barnett, G.R. and Kazarinoff, M.N. (1984) Purification and properties of ornithine decarboxylase from Physarum polycephalum. J. Biol. Chem. 259: 179-183.
    • (1984) J. Biol. Chem. , vol.259 , pp. 179-183
    • Barnett, G.R.1    Kazarinoff, M.N.2
  • 2
    • 0025616156 scopus 로고
    • Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the E. coli arginine decarboxylase and evidence of protein processing
    • Bell, E. and Malmberg, R.L. (1990) Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the E. coli arginine decarboxylase and evidence of protein processing. Mol. Gen. Genet. 224: 431-436.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 431-436
    • Bell, E.1    Malmberg, R.L.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantites of protein using the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for quantitation of microgram quantites of protein using the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0041012238 scopus 로고
    • Purification and partial characterization of arginine decarboxylase from rice embryos (Oriza saliva L.)
    • Choudhuri, M.M. and Ghosh, B. (1982) Purification and partial characterization of arginine decarboxylase from rice embryos (Oriza saliva L.). Agric. Biol. Chem. 46: 739-743.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 739-743
    • Choudhuri, M.M.1    Ghosh, B.2
  • 5
    • 0000454546 scopus 로고
    • Do polyamines have roles in plant development?
    • Evans, P.T. and Malmberg, R.L. (1989) Do polyamines have roles in plant development? Annu. Rev. Plant Physiol. 40: 235-269.
    • (1989) Annu. Rev. Plant Physiol. , vol.40 , pp. 235-269
    • Evans, P.T.1    Malmberg, R.L.2
  • 6
    • 0001834208 scopus 로고
    • Osmotic stress-induced polyamine accumulation in cereals. I. Physiological parameters of the response
    • Flores, H.E. and Galston, A.W. (1984) Osmotic stress-induced polyamine accumulation in cereals. I. Physiological parameters of the response. Plant Physiol. 75: 102-109.
    • (1984) Plant Physiol. , vol.75 , pp. 102-109
    • Flores, H.E.1    Galston, A.W.2
  • 7
    • 84989762021 scopus 로고
    • Polyamine concentrations and arginine decarboxylase activity in wheat exposed to osmotic stress
    • Foster, S.A. and Walter, D.R. (1991) Polyamine concentrations and arginine decarboxylase activity in wheat exposed to osmotic stress. Physiol. Plant. 82: 185-190.
    • (1991) Physiol. Plant. , vol.82 , pp. 185-190
    • Foster, S.A.1    Walter, D.R.2
  • 8
    • 0000508407 scopus 로고
    • Polyamines as modulators of plant development
    • Galston, A.W. (1983) Polyamines as modulators of plant development. Bioscience 33: 382-388.
    • (1983) Bioscience , vol.33 , pp. 382-388
    • Galston, A.W.1
  • 9
  • 11
    • 0028101319 scopus 로고
    • Arginine decarboxylase of oat is activated by enzymatic cleavage into two polypeptides
    • Malmberg, R.L. and Cellino, M.L. (1994) Arginine decarboxylase of oat is activated by enzymatic cleavage into two polypeptides. J. biol. Chem. 269: 2703-2707.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2703-2707
    • Malmberg, R.L.1    Cellino, M.L.2
  • 12
    • 0000424069 scopus 로고
    • Arginine decarboxylase of oat is clipped from a precursor into two polypeptides found in the soluble enzyme
    • Malmberg, R.L., Smith, K.E., Bell, E. and Cellino, M.L. (1992) Arginine decarboxylase of oat is clipped from a precursor into two polypeptides found in the soluble enzyme. Plant Physiol. 100: 146-152.
    • (1992) Plant Physiol. , vol.100 , pp. 146-152
    • Malmberg, R.L.1    Smith, K.E.2    Bell, E.3    Cellino, M.L.4
  • 13
    • 0039233714 scopus 로고
    • Some properties of arginine decarboxylase in Vicia fava leaves
    • Matsuda, H. (1984) Some properties of arginine decarboxylase in Vicia fava leaves. Plant Cell Physiol. 25: 523-530.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 523-530
    • Matsuda, H.1
  • 14
    • 0024348323 scopus 로고
    • Purification and some properties of rat intestinal ornithine decarboxylase
    • Miyamoto, K., Oka, Y., Tamaji, M., Minami, H., Nakabou, Y. and Hagihira, H. (1989) Purification and some properties of rat intestinal ornithine decarboxylase. J. Biochem. 106: 167-171.
    • (1989) J. Biochem. , vol.106 , pp. 167-171
    • Miyamoto, K.1    Oka, Y.2    Tamaji, M.3    Minami, H.4    Nakabou, Y.5    Hagihira, H.6
  • 15
    • 0001372762 scopus 로고    scopus 로고
    • A cDNA encoding arginine decarboxylase (GenBank No. U35367) from soybean hypocotyls
    • Nam, K.H., Lee, S.H. and Lee, J.H. (1996) A cDNA encoding arginine decarboxylase (GenBank No. U35367) from soybean hypocotyls. Plant Physiol. 110: 714.
    • (1996) Plant Physiol. , vol.110 , pp. 714
    • Nam, K.H.1    Lee, S.H.2    Lee, J.H.3
  • 16
    • 0008138405 scopus 로고    scopus 로고
    • Differential expression of ADC mRNA during development and upon acid stress in soybean (Glycine max) hypocotyls
    • Nam, K.H., Lee, S.H. and Lee, J.H. (1997) Differential expression of ADC mRNA during development and upon acid stress in soybean (Glycine max) hypocotyls. Plant Cell Physiol. 38: 1156-1166.
    • (1997) Plant Cell Physiol. , vol.38 , pp. 1156-1166
    • Nam, K.H.1    Lee, S.H.2    Lee, J.H.3
  • 17
    • 0029360766 scopus 로고
    • Expression of arginine decarboxylase is induced during early fruit deveolpment and in young tissue of Pisum sativum (L.)
    • Pérez-Amador, M., Carbonell, J. and Granell, A. (1995) Expression of arginine decarboxylase is induced during early fruit deveolpment and in young tissue of Pisum sativum (L.). Plant Mol. Biol. 28: 997-1009.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 997-1009
    • Pérez-Amador, M.1    Carbonell, J.2    Granell, A.3
  • 18
    • 0016820203 scopus 로고
    • Arginine decarboxylase from Lathyrus sativus seedlings
    • Ramakrishina, S. and Adiga, P.R. (1975) Arginine decarboxylase from Lathyrus sativus seedlings. Eur. J. Biochem. 59: 377-386.
    • (1975) Eur. J. Biochem. , vol.59 , pp. 377-386
    • Ramakrishina, S.1    Adiga, P.R.2
  • 19
    • 0027689369 scopus 로고
    • Cloning of tomato (Lycopersicon esculentum Mill) arginine decarboxylase gene and its expression during fruit ripening
    • Rastogi, R., Dulson, J. and Rothstein, S.J. (1993) Cloning of tomato (Lycopersicon esculentum Mill) arginine decarboxylase gene and its expression during fruit ripening. Plant Physiol. 103: 829-834.
    • (1993) Plant Physiol. , vol.103 , pp. 829-834
    • Rastogi, R.1    Dulson, J.2    Rothstein, S.J.3
  • 20
    • 0028247807 scopus 로고
    • Purification and synthesis under anaerobic conditions of rice arginine decarboxylase
    • Reggiani, R. (1994) Purification and synthesis under anaerobic conditions of rice arginine decarboxylase. Plant Cell Physiol. 35: 1245-1249.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 1245-1249
    • Reggiani, R.1
  • 21
    • 0000084708 scopus 로고
    • Relationship between the accumulation of putrescine and tolerance to oxygen-deficit stress in Gramineae seedlings
    • Reggiani, R., Giuasani, P. and Bertani, A. (1990) Relationship between the accumulation of putrescine and tolerance to oxygen-deficit stress in Gramineae seedlings Plant Cell Physiol. 31: 489-494.
    • (1990) Plant Cell Physiol. , vol.31 , pp. 489-494
    • Reggiani, R.1    Giuasani, P.2    Bertani, A.3
  • 23
    • 49249150326 scopus 로고
    • Arginine decarboxylase of oat seedlings
    • Smith, T.A. (1979) Arginine decarboxylase of oat seedlings. Phytochemistry 18: 1447-1452.
    • (1979) Phytochemistry , vol.18 , pp. 1447-1452
    • Smith, T.A.1
  • 24
    • 0001775304 scopus 로고
    • Regulation of ornithine decarboxylase and putrescine levels in Cucumis sativus cotyledons
    • Suresh, M.R., Ramakrishina, S. and Adiga, P.R. (1978) Regulation of ornithine decarboxylase and putrescine levels in Cucumis sativus cotyledons. Phytochemistry 17: 57-63.
    • (1978) Phytochemistry , vol.17 , pp. 57-63
    • Suresh, M.R.1    Ramakrishina, S.2    Adiga, P.R.3
  • 25
    • 0039233713 scopus 로고
    • Partial purification and characterization of arginine decarboxylase from avocado fruit, a thermostable enzyme
    • Winer, R., Vinkler, C. and Apelbaum, A. (1984) Partial purification and characterization of arginine decarboxylase from avocado fruit, a thermostable enzyme. Plant Physiol. 76: 233-237.
    • (1984) Plant Physiol. , vol.76 , pp. 233-237
    • Winer, R.1    Vinkler, C.2    Apelbaum, A.3
  • 26
    • 0015919380 scopus 로고
    • Biosynthetic argininedecarboxylase from Escherichia coli
    • Wu, W.H. and Morris, D.R. (1972) Biosynthetic argininedecarboxylase from Escherichia coli. J. Biol. Chem. 248: 1687-1695.
    • (1972) J. Biol. Chem. , vol.248 , pp. 1687-1695
    • Wu, W.H.1    Morris, D.R.2
  • 27
    • 0002525630 scopus 로고
    • Putrescine and acid stress
    • Young, N.D. and Galston, A.W. (1983) Putrescine and acid stress. Plant Pysiol. 71: 767-771 .
    • (1983) Plant Pysiol. , vol.71 , pp. 767-771
    • Young, N.D.1    Galston, A.W.2
  • 28
    • 0000240702 scopus 로고
    • Physiological control of arginine decarboxylase activity in potassium deficient oat shoots
    • Young, N.D. and Galston, A.W. (1984) Physiological control of arginine decarboxylase activity in potassium deficient oat shoots. Plant Physiol. 76: 331-335.
    • (1984) Plant Physiol. , vol.76 , pp. 331-335
    • Young, N.D.1    Galston, A.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.