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Volumn 30, Issue 1, 2003, Pages 88-93

Agmatine deiminase from cucumber seedlings is a mono-specific enzyme: Purification and characteristics

Author keywords

Agmatine deiminase; Cucumis sativus; Putrescine synthase

Indexed keywords

CUCUMIS; CUCUMIS SATIVUS; EMBRYOPHYTA; ZEA MAYS;

EID: 0038010125     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(03)00071-8     Document Type: Article
Times cited : (19)

References (15)
  • 2
    • 0000454546 scopus 로고
    • Do polyamines have roles in plant development?
    • P.T. Evans, R.I. Malmberg, Do polyamines have roles in plant development? Annu. Rev. Plant Physiol. 40 (1989) 235-269.
    • (1989) Annu. Rev. Plant Physiol. , vol.40 , pp. 235-269
    • Evans, P.T.1    Malmberg, R.I.2
  • 3
    • 0003092227 scopus 로고
    • Plant polyamine - Metabolism and function
    • H.E. Flores, R.N. Arteca, J.C. Shannon (Eds.), American Society of Plant Physiologists, Rockville, MD
    • T.A. Smith, Plant polyamine - metabolism and function, in: H.E. Flores, R.N. Arteca, J.C. Shannon (Eds.), Polyamines and Ethylene: Biochemistry, Physiology and Interactions, American Society of Plant Physiologists, Rockville, MD, 1990, pp. 1-23.
    • (1990) Polyamines and Ethylene: Biochemistry, Physiology and Interactions , pp. 1-23
    • Smith, T.A.1
  • 4
    • 0005266533 scopus 로고
    • Agmatine iminohydrolase in maize
    • T.A. Smith, Agmatine iminohydrolase in maize, Phytochemistry 8 (1969) 2111-2117.
    • (1969) Phytochemistry , vol.8 , pp. 2111-2117
    • Smith, T.A.1
  • 5
    • 0035815341 scopus 로고    scopus 로고
    • Agmatine deiminase from maize shoots: Purification and properties
    • H. Yanagisawa, Agmatine deiminase from maize shoots: purification and properties, Phytochemistry 56 (2001) 643-647.
    • (2001) Phytochemistry , vol.56 , pp. 643-647
    • Yanagisawa, H.1
  • 6
    • 0001457743 scopus 로고
    • Agmatine deiminase in rice seedlings
    • M.M. Chaudhuri, B. Gosh, Agmatine deiminase in rice seedlings, Phytochemistry 24 (1985) 2433-2435.
    • (1985) Phytochemistry , vol.24 , pp. 2433-2435
    • Chaudhuri, M.M.1    Gosh, B.2
  • 7
    • 0026027549 scopus 로고
    • Purification of monomeric agmatine iminohydrolase from soybean
    • K.H. Park, Y.D. Cho, Purification of monomeric agmatine iminohydrolase from soybean, Biochem. Biophys. Res. Commun. 174 (1990) 32-36.
    • (1990) Biochem. Biophys. Res. Commun. , vol.174 , pp. 32-36
    • Park, K.H.1    Cho, Y.D.2
  • 8
    • 0019888406 scopus 로고
    • Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings
    • K.S. Srivenugopal, P.R. Adiga, Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings, J. Biol. Chem. 256 (1981) 9532-9541.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9532-9541
    • Srivenugopal, K.S.1    Adiga, P.R.2
  • 9
    • 51249174504 scopus 로고
    • Purification and characterization of putrescine synthase from cucumber seedlings. A multifunctional enzyme involved in putrescine biosynthesis
    • G.L. Prasad, P.R. Adiga, Purification and characterization of putrescine synthase from cucumber seedlings. A multifunctional enzyme involved in putrescine biosynthesis, J. Biosci. 10 (1986) 373-391.
    • (1986) J. Biosci. , vol.10 , pp. 373-391
    • Prasad, G.L.1    Adiga, P.R.2
  • 10
    • 0002561651 scopus 로고
    • N-Carbamylputrescine. An intermediate in the formation of putrescine by barley
    • T.A. Smith, J.L. Garraway, N-Carbamylputrescine. An intermediate in the formation of putrescine by barley, Phytochemistry 3 (1964) 23-26.
    • (1964) Phytochemistry , vol.3 , pp. 23-26
    • Smith, T.A.1    Garraway, J.L.2
  • 11
    • 0017811513 scopus 로고
    • Formation of n-carbamyl putrescine from citrulline in Escherichia coli
    • N. Akamatsu, M. Oguchi, Y. Yajima, N. Ohno, Formation of n-carbamyl putrescine from citrulline in Escherichia coli, J. Bacteriol. 133 (1978) 409-410.
    • (1978) J. Bacteriol. , vol.133 , pp. 409-410
    • Akamatsu, N.1    Oguchi, M.2    Yajima, Y.3    Ohno, N.4
  • 12
    • 0016193169 scopus 로고
    • Adrenergic receptors and binding proteins
    • D.S. O'Hara, R.J. Lefkowitz, Adrenergic receptors and binding proteins, Methods Enzymol. 34 (1974) 695-700.
    • (1974) Methods Enzymol. , vol.34 , pp. 695-700
    • O'Hara, D.S.1    Lefkowitz, R.J.2
  • 13
    • 0019170507 scopus 로고
    • Optimization of conditions for the colorimetric determination of citrulline, using diacetyl monoxime
    • T.R.C. Boyde, M. Rahmatullah, Optimization of conditions for the colorimetric determination of citrulline, using diacetyl monoxime, Anal. Biochem. 107 (1980) 424-431.
    • (1980) Anal. Biochem. , vol.107 , pp. 424-431
    • Boyde, T.R.C.1    Rahmatullah, M.2
  • 14
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • A. Bensadoun, D. Weinstein, Assay of proteins in the presence of interfering materials, Anal. Biochem. 70 (1976) 241-250.
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.