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Volumn 53, Issue 2, 1997, Pages 226-231

Bacitracin significantly reduces degradation of peptides in plant cell cultures

Author keywords

bacitracin; peptide; plant cell culture; protease

Indexed keywords

COMPOSITION EFFECTS; DEGRADATION; ENZYMES; PLANT CELL CULTURE;

EID: 0031021810     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19970120)53:2<226::AID-BIT14>3.0.CO;2-I     Document Type: Article
Times cited : (14)

References (30)
  • 1
    • 0027388885 scopus 로고
    • Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-dependent protein degradation
    • USA
    • Bachmair, A., Becker, F., Schell, J. 1993. Use of a reporter transgene to generate Arabidopsis mutants in ubiquitin-dependent protein degradation. Proc. Natl. Acad. Sci. USA 90: 418-421.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 418-421
    • Bachmair, A.1    Becker, F.2    Schell, J.3
  • 2
    • 84989711468 scopus 로고
    • Physiological and biochemical characterization of a suspension-culture system for sustained exponential growth of Nicotiana silvestris
    • Bonner, C. A., Kenyon, C., Jensen, R. A. 1988. Physiological and biochemical characterization of a suspension-culture system for sustained exponential growth of Nicotiana silvestris. Physiol. Plant. 74: 1-10.
    • (1988) Physiol. Plant. , vol.74 , pp. 1-10
    • Bonner, C.A.1    Kenyon, C.2    Jensen, R.A.3
  • 3
    • 0027508505 scopus 로고
    • Secretion of heterologous proteins by Aspergillus niger: Production of active human interleukin-6 in a protease-deficient mutant by KEX2-like processing of a glucoamylase-hIL6 fusion protein
    • Broekhuijsen, M. P., Mattem, I. E., Contreras, R., Kinghorn, J. R., van den Hondel, C. A. M. J. J. 1993. Secretion of heterologous proteins by Aspergillus niger: Production of active human interleukin-6 in a protease-deficient mutant by KEX2-like processing of a glucoamylase-hIL6 fusion protein. J. Biotechnol. 31: 135-145.
    • (1993) J. Biotechnol. , vol.31 , pp. 135-145
    • Broekhuijsen, M.P.1    Mattem, I.E.2    Contreras, R.3    Kinghorn, J.R.4    Van Den Hondel, C.A.M.J.J.5
  • 4
    • 0015978423 scopus 로고
    • Inhibitors of glucagon inactivation. Effect on glucagon-receptor interactions and glucagon-stimulated adenylate cyclase activity in liver cell membranes
    • Desbuquois, B., Krug, F., Cuatrecasas, P. 1974. Inhibitors of glucagon inactivation. Effect on glucagon-receptor interactions and glucagon-stimulated adenylate cyclase activity in liver cell membranes. Biochim. Biophys. Acta 343: 101-120.
    • (1974) Biochim. Biophys. Acta , vol.343 , pp. 101-120
    • Desbuquois, B.1    Krug, F.2    Cuatrecasas, P.3
  • 5
    • 1842397667 scopus 로고
    • Bacitracin inhibits the synthesis of lipid-linked saccharides and glycoproteins in plants
    • Ericson, M. C., Gafford, J., Elbein, A. D. 1978. Bacitracin inhibits the synthesis of lipid-linked saccharides and glycoproteins in plants. Plant Physiol. 62: 373-376.
    • (1978) Plant Physiol. , vol.62 , pp. 373-376
    • Ericson, M.C.1    Gafford, J.2    Elbein, A.D.3
  • 6
    • 0019799112 scopus 로고
    • Calcitonin binding and degradation by two cultured human breast cancer cell lines (MCF 7 and T 47D)
    • Findlay, D. M., Michelangeli, V. P., Moseley, J. M., Martin, T. J. 1981. Calcitonin binding and degradation by two cultured human breast cancer cell lines (MCF 7 and T 47D). Biochem. J. 196: 513-520.
    • (1981) Biochem. J. , vol.196 , pp. 513-520
    • Findlay, D.M.1    Michelangeli, V.P.2    Moseley, J.M.3    Martin, T.J.4
  • 7
    • 0003118603 scopus 로고
    • The induction of nitrogenase activity in Rhizobium by non-legume plant cells
    • Gibson, A. H., Child, J. J., Pagan, J. D., Scowcroft, W. R. 1976. The induction of nitrogenase activity in Rhizobium by non-legume plant cells. Planta 128: 233-239.
    • (1976) Planta , vol.128 , pp. 233-239
    • Gibson, A.H.1    Child, J.J.2    Pagan, J.D.3    Scowcroft, W.R.4
  • 8
    • 14744286826 scopus 로고
    • A new tobacco mosaic virus vector and its use for the systemic production of angiotensin-I-converting enzyme inhibitor in transgenic tobacco and tomato
    • Hamamoto, H., Sugiyama, Y., Nakagawa, N., Hashida, E., Matsunaga, Y., Takemoto, S., Watanabe, Y., Okada, Y. 1993. A new tobacco mosaic virus vector and its use for the systemic production of angiotensin-I-converting enzyme inhibitor in transgenic tobacco and tomato. Bio/Technology 11: 930-932.
    • (1993) Bio/Technology , vol.11 , pp. 930-932
    • Hamamoto, H.1    Sugiyama, Y.2    Nakagawa, N.3    Hashida, E.4    Matsunaga, Y.5    Takemoto, S.6    Watanabe, Y.7    Okada, Y.8
  • 9
    • 0020360441 scopus 로고
    • 125I-insulin is associated with an increase in plasma membrane bound insulin and a potentiation of glucose oxidation by adipocytes
    • 125I-insulin is associated with an increase in plasma membrane bound insulin and a potentiation of glucose oxidation by adipocytes. J. Biol. Chem. 257: 11563-11570.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11563-11570
    • Hammons, G.T.1    Smith, R.M.2    Jarett, L.3
  • 10
    • 0027254862 scopus 로고
    • Effect of arginine vasopressin and parathyroid hormone-related protein on renal function in the ovine foetus
    • Horne, R. S. C., MacIsaac, R. J., Moritz, K. M., Tangalakis, K., Wintour, E. M. 1993. Effect of arginine vasopressin and parathyroid hormone-related protein on renal function in the ovine foetus. Clin. Exp. Pharmacol. Physiol. 20: 569-577.
    • (1993) Clin. Exp. Pharmacol. Physiol. , vol.20 , pp. 569-577
    • Horne, R.S.C.1    MacIsaac, R.J.2    Moritz, K.M.3    Tangalakis, K.4    Wintour, E.M.5
  • 11
    • 0345174432 scopus 로고
    • Principles of protein turnover: Possible manipulations
    • A. R. Rees, M. J. E. Sternberg, and R. Wetzel (eds.), Oxford University Press, Oxford
    • Jentsch, S., Bachmair, A. 1992. Principles of protein turnover: possible manipulations, pp. 221-228. In: A. R. Rees, M. J. E. Sternberg, and R. Wetzel (eds.), Protein engineering: a practical approach. Oxford University Press, Oxford.
    • (1992) Protein Engineering: A Practical Approach , pp. 221-228
    • Jentsch, S.1    Bachmair, A.2
  • 12
    • 84940980742 scopus 로고
    • Structure and biosynthesis of plant N-linked glycoproteins
    • J. Preiss (ed.), Academic Press, San Diego, CA
    • Kaushal, G. P., Szumilo, T., Elbein, A. D. 1988. Structure and biosynthesis of plant N-linked glycoproteins, pp. 421-463. In: J. Preiss (ed.), The biochemistry of plants, vol. 14. Academic Press, San Diego, CA.
    • (1988) The Biochemistry of Plants , vol.14 , pp. 421-463
    • Kaushal, G.P.1    Szumilo, T.2    Elbein, A.D.3
  • 15
    • 0023644824 scopus 로고
    • Structure and expression of an alcohol dehydrogenase 1 gene from Pisum sativum (cv. "Greenfeast")
    • Llewellyn, D. J., Finnegan, E. J., Ellis, J. G., Dennis, E. S., Peacock, W. J. 1987. Structure and expression of an alcohol dehydrogenase 1 gene from Pisum sativum (cv. "Greenfeast"). J. Mol. Biol. 195: 115-123.
    • (1987) J. Mol. Biol. , vol.195 , pp. 115-123
    • Llewellyn, D.J.1    Finnegan, E.J.2    Ellis, J.G.3    Dennis, E.S.4    Peacock, W.J.5
  • 17
    • 1842394733 scopus 로고
    • Effect of various media on growth and protease production in Carica papaya L. callus cultures
    • Medora, R. S., Mell, G. P., Bilderback, D. E. 1984. Effect of various media on growth and protease production in Carica papaya L. callus cultures. Z. Pflanzenphysiol. 114: 179-185.
    • (1984) Z. Pflanzenphysiol. , vol.114 , pp. 179-185
    • Medora, R.S.1    Mell, G.P.2    Bilderback, D.E.3
  • 18
    • 0028143313 scopus 로고
    • Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins
    • Meerman, H. J., Georgiou, G. 1994. Construction and characterization of a set of E. coli strains deficient in all known loci affecting the proteolytic stability of secreted recombinant proteins. Bio/Technology 12: 1107-1110.
    • (1994) Bio/Technology , vol.12 , pp. 1107-1110
    • Meerman, H.J.1    Georgiou, G.2
  • 19
    • 85025524677 scopus 로고
    • Ficin production by callus cultures of Ficus carica
    • Nassar, A. H., Newbury, H. J. 1987. Ficin production by callus cultures of Ficus carica. J. Plant Physiol. 131: 171-179.
    • (1987) J. Plant Physiol. , vol.131 , pp. 171-179
    • Nassar, A.H.1    Newbury, H.J.2
  • 20
    • 0019421249 scopus 로고
    • Bacitracin: An inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase
    • Roth, R. A. 1981. Bacitracin: an inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase. Biochem. Biophys. Res. Commun. 98: 431-438.
    • (1981) Biochem. Biophys. Res. Commun. , vol.98 , pp. 431-438
    • Roth, R.A.1
  • 21
    • 0345665954 scopus 로고
    • Multiple joined genes prevent product degradation in Escherichia coli
    • USA
    • Shen, S. H. 1984. Multiple joined genes prevent product degradation in Escherichia coli. Proc. Nat. Acad. Sci. USA 81: 4627-4631.
    • (1984) Proc. Nat. Acad. Sci. , vol.81 , pp. 4627-4631
    • Shen, S.H.1
  • 22
    • 1842388877 scopus 로고
    • Bacitracin
    • F. E. Hahn (ed.), Springer, Berlin
    • Storm, D. R., Toscano, W. A., Jr. 1979. Bacitracin, pp. 1-17. In: F. E. Hahn (ed.), Antibiotics, vol. 5, part 1. Springer, Berlin.
    • (1979) Antibiotics , vol.5 , Issue.1 PART , pp. 1-17
    • Storm, D.R.1    Toscano Jr., W.A.2
  • 23
    • 0025125026 scopus 로고
    • Production of enkephalin in tobacco protoplasts using tobacco mosaic virus RNA vector
    • Takamatsu, N., Watanabe, Y., Yanagi, H., Meshi, T., Shiba, T., Okada, Y. 1990. Production of enkephalin in tobacco protoplasts using tobacco mosaic virus RNA vector. FEBS Lett. 269: 73-76.
    • (1990) FEBS Lett. , vol.269 , pp. 73-76
    • Takamatsu, N.1    Watanabe, Y.2    Yanagi, H.3    Meshi, T.4    Shiba, T.5    Okada, Y.6
  • 24
    • 38249036755 scopus 로고
    • Effect of inorganic phosphate on the levels of amino acids in suspension-cultured cells of Catharanthus roseus
    • London
    • Ukaji, T., Ashihara, H. 1987. Effect of inorganic phosphate on the levels of amino acids in suspension-cultured cells of Catharanthus roseus. Ann. Bot. (London) 60: 109-114.
    • (1987) Ann. Bot. , vol.60 , pp. 109-114
    • Ukaji, T.1    Ashihara, H.2
  • 26
    • 0026094571 scopus 로고
    • Visualization of proteases within a complex sample following their selective retention on immobilized bacitracin, a peptide antibiotic
    • van Noort, J. M., van den Berg, P., Mattern, I. E. 1991. Visualization of proteases within a complex sample following their selective retention on immobilized bacitracin, a peptide antibiotic. Anal. Biochem. 198: 385-390.
    • (1991) Anal. Biochem. , vol.198 , pp. 385-390
    • Van Noort, J.M.1    Van Den Berg, P.2    Mattern, I.E.3
  • 27
    • 0000790802 scopus 로고
    • Evidence for an extracellular lytic compartment of plant cell suspension cultures: The cell culture medium
    • Wink, M. 1984. Evidence for an extracellular lytic compartment of plant cell suspension cultures: the cell culture medium. Naturwissenschaften 71: 635-637.
    • (1984) Naturwissenschaften , vol.71 , pp. 635-637
    • Wink, M.1
  • 28
    • 0041585027 scopus 로고
    • Composition of the spent cell culture medium. I. Time-course of ethanol formation and the excretion of hydrolytic enzymes into the medium of suspension-cultured cells of Lupinus polyphyllus
    • Wink, M. 1985. Composition of the spent cell culture medium. I. Time-course of ethanol formation and the excretion of hydrolytic enzymes into the medium of suspension-cultured cells of Lupinus polyphyllus. J. Plant Physiol. 121: 287-293.
    • (1985) J. Plant Physiol. , vol.121 , pp. 287-293
    • Wink, M.1
  • 29
    • 0000279196 scopus 로고
    • The cell culture medium - A functional extracellular compartment of suspension-cultured cells
    • Wink, M. 1994. The cell culture medium - a functional extracellular compartment of suspension-cultured cells. Plant Cell, Tissue Organ Cult. 38: 307-319.
    • (1994) Plant Cell, Tissue Organ Cult. , vol.38 , pp. 307-319
    • Wink, M.1
  • 30
    • 1842401862 scopus 로고
    • Enzymatic difference between laticifers and cultured cells of papaya
    • Yamamoto, H., Tanaka, S., Fukui, H., Tabata, M. 1986. Enzymatic difference between laticifers and cultured cells of papaya. Plant Cell Rep. 5: 269-272.
    • (1986) Plant Cell Rep. , vol.5 , pp. 269-272
    • Yamamoto, H.1    Tanaka, S.2    Fukui, H.3    Tabata, M.4


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