메뉴 건너뛰기




Volumn 37, Issue 4, 2010, Pages 1823-1829

Expression and purification of recombinant arginine decarboxylase (speA) from Escherichia coli

Author keywords

Arginine decarboxylase (ADC); Enzyme activity characterization; Expression; Purification; SpeA

Indexed keywords

ARGININE; ARGININE DECARBOXYLASE; HISTIDINE; POLYHISTIDINE; PROTEINASE; RECOMBINANT ENZYME; CARBOXYLYASE; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN;

EID: 77953169200     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-009-9617-0     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 0032533159 scopus 로고    scopus 로고
    • Arginine metabolism: Nitric oxide and beyond
    • Wu G, Morris SM Jr (1998) Arginine metabolism: nitric oxide and beyond. Biochem J 336:1-17
    • (1998) Biochem J , vol.336 , pp. 1-17
    • Wu, G.1    Morris Jr., S.M.2
  • 2
    • 2542527672 scopus 로고    scopus 로고
    • Putrescine biosynthesis in mammalian tissues
    • Coleman CS, Hu G, Pegg AE (2004) Putrescine biosynthesis in mammalian tissues. Biochem J 379:849-855
    • (2004) Biochem J , vol.379 , pp. 849-855
    • Coleman, C.S.1    Hu, G.2    Pegg, A.E.3
  • 3
    • 1642450643 scopus 로고    scopus 로고
    • Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine
    • Zhu MY, Iyo A, Piletz JE et al (2004) Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine. Biochim Biophys Acta 1670:156-164
    • (2004) Biochim Biophys Acta , vol.1670 , pp. 156-164
    • Zhu, M.Y.1    Iyo, A.2    Piletz, J.E.3
  • 4
    • 0030911495 scopus 로고    scopus 로고
    • Determination of agmatine in brain and plasma using high-performance liquid chromatography with fluorescence detection
    • Feng Y, Halaris AE, Piletz JE (1997) Determination of agmatine in brain and plasma using high-performance liquid chromatography with fluorescence detection. J. Chromatogr. B Biomed. Sci. Appl. 691:277-286
    • (1997) J. Chromatogr. B Biomed. Sci. Appl , vol.691 , pp. 277-286
    • Feng, Y.1    Halaris, A.E.2    Piletz, J.E.3
  • 5
    • 34548003048 scopus 로고    scopus 로고
    • Agmatine: A novel neurotransmitter?
    • Reis DJ, Regunathan S (1998) Agmatine: A novel neurotransmitter? Adv Pharmacol 42:645-649
    • (1998) Adv Pharmacol , vol.42 , pp. 645-649
    • Reis, D.J.1    Regunathan, S.2
  • 6
    • 0030098067 scopus 로고    scopus 로고
    • Imidazoline receptors and agmatine in blood vessels: A novel system inhibiting vascular smooth muscle proliferation
    • Regunathan S, Youngson C, Raasch W et al (1996) Imidazoline receptors and agmatine in blood vessels: A novel system inhibiting vascular smooth muscle proliferation. J Pharmacol Exp Ther 276:1272-1282
    • (1996) J Pharmacol Exp Ther , vol.276 , pp. 1272-1282
    • Regunathan, S.1    Youngson, C.2    Raasch, W.3
  • 7
    • 0032546959 scopus 로고    scopus 로고
    • Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels
    • Satriano J, Matsufuji S, Murakami Y et al (1998) Agmatine suppresses proliferation by frameshift induction of antizyme and attenuation of cellular polyamine levels. J Biol Chem 273:15313-15316
    • (1998) J Biol Chem , vol.273 , pp. 15313-15316
    • Satriano, J.1    Matsufuji, S.2    Murakami, Y.3
  • 8
    • 0032796565 scopus 로고    scopus 로고
    • Anti-proliferative and anti-inflammatory actions of imidazoline agents. Are imidazoline receptors involved?
    • Regunathan S, Feinstein DL, Reis DJ (1999) Anti-proliferative and anti-inflammatory actions of imidazoline agents. Are imidazoline receptors involved? Ann N Y Acad Sci 881:410-419
    • (1999) Ann N Y Acad Sci , vol.881 , pp. 410-419
    • Regunathan, S.1    Feinstein, D.L.2    Reis, D.J.3
  • 10
    • 0034685624 scopus 로고    scopus 로고
    • Polyamines: Mysterious modulators of cellular functions
    • Igarashi K, Kashiwagi K (2000) Polyamines: mysterious modulators of cellular functions. Biochem Biophys Res Commun 271:559-564
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 559-564
    • Igarashi, K.1    Kashiwagi, K.2
  • 11
    • 0033634723 scopus 로고    scopus 로고
    • A cell cycledependent internal ribosome entry site
    • Pyronnet S, Pradayrol L, Sonenberg N (2000) A cell cycledependent internal ribosome entry site. Mol. Cell 5:607-616
    • (2000) Mol. Cell , vol.5 , pp. 607-616
    • Pyronnet, S.1    Pradayrol, L.2    Sonenberg, N.3
  • 12
    • 0014670057 scopus 로고
    • Formation of 1, 4-diaminobutane and of spermidine by an ornithine auxotroph of Escherichia coli grown on limiting ornithine or arginine
    • Tabor H, Tabor CW (1969) Formation of 1, 4-diaminobutane and of spermidine by an ornithine auxotroph of Escherichia coli grown on limiting ornithine or arginine. J Biol Chem 244:2286-2292
    • (1969) J Biol Chem , vol.244 , pp. 2286-2292
    • Tabor, H.1    Tabor, C.W.2
  • 13
    • 0020123564 scopus 로고
    • Membrane-filter technique for the isolation of Yersinia enterocolitica
    • Bartley TD, Quan TJ, Collins MT et al (1982) Membrane-filter technique for the isolation of Yersinia enterocolitica. Appl Environ Microbiol 43:829-834
    • (1982) Appl Environ Microbiol , vol.43 , pp. 829-834
    • Bartley, T.D.1    Quan, T.J.2    Collins, M.T.3
  • 14
    • 0020651628 scopus 로고
    • Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli
    • Morris DR, Boeker EA (1983) Biosynthetic and biodegradative ornithine and arginine decarboxylases from Escherichia coli. Methods Enzymol 94:125-134
    • (1983) Methods Enzymol , vol.94 , pp. 125-134
    • Morris, D.R.1    Boeker, E.A.2
  • 15
    • 0025616156 scopus 로고
    • Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing
    • Bell E, Malmberg RL (1990) Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia 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
  • 16
    • 0015919380 scopus 로고
    • Biosynthetic arginine decarboxylase from Escherichia coli: Purification and properties
    • Wu WH, Morris DR (1973) Biosynthetic arginine decarboxylase from Escherichia coli: purification and properties. J Biol Chem 248:1687-1695
    • (1973) J Biol Chem , vol.248 , pp. 1687-1695
    • Wu, W.H.1    Morris, D.R.2
  • 17
    • 0016139395 scopus 로고
    • Regulation of amino acid decarboxylation
    • Morris DR, Fillingame RH (1974) Regulation of amino acid decarboxylation. Annu Rev Biochem 43:303-325
    • (1974) Annu Rev Biochem , vol.43 , pp. 303-325
    • Morris, D.R.1    Fillingame, R.H.2
  • 18
    • 0021884143 scopus 로고
    • Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope
    • Buch JK, Boyle SM (1985) Biosynthetic arginine decarboxylase in Escherichia coli is synthesized as a precursor and located in the cell envelope. J Bacteriol 163:522-527
    • (1985) J Bacteriol , vol.163 , pp. 522-527
    • Buch, J.K.1    Boyle, S.M.2
  • 19
    • 0014670919 scopus 로고
    • Partial separation of two pools of arginine in Escherichia coli; preferential use of exogenous rather than endogenous arginine for the biosynthesis of 1, 4-diaminobutane
    • Tabor H, Tabor CW (1969) Partial separation of two pools of arginine in Escherichia coli; preferential use of exogenous rather than endogenous arginine for the biosynthesis of 1, 4-diaminobutane. J Biol Chem 244:6383-6387
    • (1969) J Biol Chem , vol.244 , pp. 6383-6387
    • Tabor, H.1    Tabor, C.W.2
  • 20
    • 0020360530 scopus 로고
    • Negative control of ornithine decarboxylase and arginine decarboxylase by adenosine-30:50-cyclic monophosphate in Escherichia coli
    • Wright JM, Boyle SM (1982) Negative control of ornithine decarboxylase and arginine decarboxylase by adenosine-30:50- cyclic monophosphate in Escherichia coli. Mol Gen Genet 186:482-487
    • (1982) Mol Gen Genet , vol.186 , pp. 482-487
    • Wright, J.M.1    Boyle, S.M.2
  • 21
    • 0008138405 scopus 로고    scopus 로고
    • Differential expression of ADC mRNA during development and upon acid stress in soybean (Glycine max) hypocotyls
    • Nam KH, Lee SH, Lee J (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.3
  • 22
    • 0033775991 scopus 로고    scopus 로고
    • Characterization and translational regulation of the arginine decarboxylase gene in carnation (Dianthus caryophyllus L.)
    • Chang KS, Lee SH, Hwang SB et al (2000) Characterization and translational regulation of the arginine decarboxylase gene in carnation (Dianthus caryophyllus L.). Plant J 24:45-56
    • (2000) Plant J , vol.24 , pp. 45-56
    • Chang, K.S.1    Lee, S.H.2    Hwang, S.B.3
  • 23
    • 0034798209 scopus 로고    scopus 로고
    • Arabidopsis polyamine biosynthesis: Absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity
    • Hanfrey C, Sommer S, Mayer MJ et al (2001) Arabidopsis polyamine biosynthesis: Absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity. Plant J 27:551-560
    • (2001) Plant J , vol.27 , pp. 551-560
    • Hanfrey, C.1    Sommer, S.2    Mayer, M.J.3
  • 24
    • 0016820203 scopus 로고
    • Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properties
    • Ramakrishna S, Adiga PR (1975) Arginine decarboxylase from Lathyrus sativus seedlings. Purification and properties. Eur J Biochem 59:377-386
    • (1975) Eur J Biochem , vol.59 , pp. 377-386
    • Ramakrishna, S.1    Adiga, P.R.2
  • 25
    • 49249150326 scopus 로고
    • Arginine decarboxylase of oat seedlings
    • Smith TA (1979) Arginine decarboxylase of oat seedlings. Phytochemistry 18:1447-1452
    • (1979) Phytochemistry , vol.18 , pp. 1447-1452
    • Smith, T.A.1
  • 26
    • 0343738429 scopus 로고
    • Purification and properties of l-arginine decarboxylase of Evernia prunastri
    • Vicente C, Legaz E (1981) Purification and properties of l-arginine decarboxylase of Evernia prunastri. Plant Cell Physiol 22:1119-1123
    • (1981) Plant Cell Physiol , vol.22 , pp. 1119-1123
    • Vicente, C.1    Legaz, E.2
  • 27
    • 0041012238 scopus 로고
    • Purification and partial characterization of arginine decarboxylase from rice embryos (Oryza sativa L.)
    • Choudhuri MM, Ghosh B (1982) Purification and partial characterization of arginine decarboxylase from rice embryos (Oryza sativa L.). Agric. Biol. Chem 46:739-743
    • (1982) Agric. Biol. Chem , vol.46 , pp. 739-743
    • Choudhuri, M.M.1    Ghosh, B.2
  • 28
    • 0039233713 scopus 로고
    • Partial-purification and characterization of arginine decarboxylase from avocado fruit, a thermostable enzyme
    • Winer L, Vinkler C, 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, L.1    Vinkler, C.2    Apelbaum, A.3
  • 29
    • 51649149238 scopus 로고
    • Purification and characterization of arginine decarboxylase from cucumber (cucumis sativus) seedlings
    • Prasad GL, Adiga PR (1985) Purification and characterization of arginine decarboxylase from cucumber (cucumis sativus) seedlings. J Biosci 7:331-343
    • (1985) J Biosci , vol.7 , pp. 331-343
    • Prasad, G.L.1    Adiga, P.R.2
  • 30
    • 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
  • 31
    • 0042643038 scopus 로고    scopus 로고
    • Purification and partial characterization of arginine decarboxylase from Brassica campestris
    • Das S, Bhaduri TJ, Bose A et al (1996) Purification and partial characterization of arginine decarboxylase from Brassica campestris. J Plant Biochem Biotechnol 5:123-126
    • (1996) J Plant Biochem Biotechnol , vol.5 , pp. 123-126
    • Das, S.1    Bhaduri, T.J.2    Bose, A.3
  • 32
    • 2342557362 scopus 로고    scopus 로고
    • Characterization of arginine decarboxylase from Dianthus caryophyllus
    • Ha BH, Cho KJ, Choi YJ et al (2004) Characterization of arginine decarboxylase from Dianthus caryophyllus. Plant Physiol Biochem 42:307-311
    • (2004) Plant Physiol Biochem , vol.42 , pp. 307-311
    • Ha, B.H.1    Cho, K.J.2    Choi, Y.J.3
  • 33
    • 1642332949 scopus 로고    scopus 로고
    • Expression and purification of recombinant cytoplasmic domain of human erythrocyte band 3 with hexahistidine tag or chitin-binding tag in Escherichia coli
    • Ding Y, Jiang W, Su Y et al (2004) Expression and purification of recombinant cytoplasmic domain of human erythrocyte band 3 with hexahistidine tag or chitin-binding tag in Escherichia coli. Protein Expr Purif 34:167-175
    • (2004) Protein Expr Purif , vol.34 , pp. 167-175
    • Ding, Y.1    Jiang, W.2    Su, Y.3
  • 34
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41:207-234
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 35
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by directed evolution
    • van den Berg S, Lofdahl PA, Hard T et al (2006) Improved solubility of TEV protease by directed evolution. J Biotechnol 121:291-298
    • (2006) J Biotechnol , vol.121 , pp. 291-298
    • Van Den, B.S.1    Lofdahl, P.A.2    Hard, T.3
  • 36
    • 0015116353 scopus 로고
    • Simplified rapid procedure for determination of agmatine and other guanidino-containing compounds
    • Goldschmidt MC, Lockhart BM (1971) Simplified rapid procedure for determination of agmatine and other guanidino-containing compounds. Anal Chem 43:1475-1479
    • (1971) Anal Chem , vol.43 , pp. 1475-1479
    • Goldschmidt, M.C.1    Lockhart, B.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.