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Volumn 155, Issue 4-5, 1999, Pages 462-469

A novel β-glucosidase from the cell wall of maize (Zea mays L.): Rapid purification and partial characterization

Author keywords

Cell wall; Coleoptile; Enzyme kinetics; Maize; Mesocotyl; Monoclonal antibody; Peroxidase; Red light; Zea mays L.; Glucosidase

Indexed keywords

BETA GLUCOSIDASE; CELL WALL; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION;

EID: 0032750603     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0176-1617(99)80040-6     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • BRADFORD, M. M. A.: A rapid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.A.1
  • 2
    • 0027738757 scopus 로고
    • Release of active cytokinin by a β-glucosidase localized to the maize root meristem
    • BRZOBOHATÝ, B., I. MOORE, P. KRISTOFFERSEN, L. BAKO, N. CAMPOS, J. SCHELL, and K. PALME: Release of active cytokinin by a β-glucosidase localized to the maize root meristem. Science 262, 1051-1054 (1993).
    • (1993) Science , vol.262 , pp. 1051-1054
    • Brzobohatý, B.1    Moore, I.2    Kristoffersen, P.3    Bako, L.4    Campos, N.5    Schell, J.6    Palme, K.7
  • 3
    • 0027249595 scopus 로고
    • dbEST: Database for «expressed sequence tags»
    • BOGUSKI, M. S., T. M. J. LOWE, and C. M. TOLSTOSHEV: dbEST: database for «expressed sequence tags». Nature Genet. 4, 332-333 (1993).
    • (1993) Nature Genet. , vol.4 , pp. 332-333
    • Boguski, M.S.1    Lowe, T.M.J.2    Tolstoshev, C.M.3
  • 4
    • 0000878877 scopus 로고
    • A protein from maize labeled with azido-IAA has novel β-glucosidase activity
    • CAMPOS, N., L. BAKO, J. FELDWISCH, J. SCHELL, and K. PALME: A protein from maize labeled with azido-IAA has novel β-glucosidase activity. Plant J. 2, 675-684 (1992).
    • (1992) Plant J. , vol.2 , pp. 675-684
    • Campos, N.1    Bako, L.2    Feldwisch, J.3    Schell, J.4    Palme, K.5
  • 5
    • 0001506290 scopus 로고
    • Partial purification and characterization of a hydroxamic acid glucoside β-D-glucosidase from maize
    • CUEVAS, L., H. M. NIEMEYER, and L. M. V. JONSSON: Partial purification and characterization of a hydroxamic acid glucoside β-D-glucosidase from maize. Phytochemistry 31, 2609-2612 (1992).
    • (1992) Phytochemistry , vol.31 , pp. 2609-2612
    • Cuevas, L.1    Niemeyer, H.M.2    Jonsson, L.M.V.3
  • 6
    • 0002075691 scopus 로고
    • Characterization and localization of laccase forms in stem and cell cultures of sycamore
    • DRIOUICH, A., A.-C. LAINÉ, B. VIAN, and L. FAYE: Characterization and localization of laccase forms in stem and cell cultures of sycamore. Plant J. 2, 13-24 (1992).
    • (1992) Plant J. , vol.2 , pp. 13-24
    • Driouich, A.1    Lainé, A.-C.2    Vian, B.3    Faye, L.4
  • 7
    • 0030801737 scopus 로고    scopus 로고
    • Compounds exuded by Phaseolus vulgaris that induce a modification of Rhizobium etli lipopolysaccharide
    • DUELLI, D. M. and K. D. NOEL: Compounds exuded by Phaseolus vulgaris that induce a modification of Rhizobium etli lipopolysaccharide. Molec. Plant-Microbe Interact. 10, 903-910 (1997).
    • (1997) Molec. Plant-Microbe Interact. , vol.10 , pp. 903-910
    • Duelli, D.M.1    Noel, K.D.2
  • 8
    • 0000198169 scopus 로고
    • Purification and partial characterization of maize (Zea mays L.) β-glucosidase
    • ESEN, A.: Purification and partial characterization of maize (Zea mays L.) β-glucosidase. Plant Physiol. 98, 174-182 (1992).
    • (1992) Plant Physiol. , vol.98 , pp. 174-182
    • Esen, A.1
  • 9
    • 0343460407 scopus 로고
    • pH- and temperature-dependent β-glucosidase multiplicity in maize (Zea mays L.) is a proteolysis artifact
    • ESEN, A. and C. COKUMS [sic; Çokmuş]: pH- and temperature-dependent β-glucosidase multiplicity in maize (Zea mays L.) is a proteolysis artifact. Plant Sci. 74, 17-26 (1991).
    • (1991) Plant Sci. , vol.74 , pp. 17-26
    • Esen, A.1    Cokums, C.2
  • 10
    • 0022417293 scopus 로고
    • The action of auxin on plant cell elongation
    • EVANS, M. L.: The action of auxin on plant cell elongation. CRC Crit. Rev. Plant Sci. 2, 317-365 (1985).
    • (1985) CRC Crit. Rev. Plant Sci. , vol.2 , pp. 317-365
    • Evans, M.L.1
  • 11
    • 0025215437 scopus 로고
    • Spinach carbonic anhydrase primary structure deduced from the sequence of a cDNA clone
    • FAWCETT, T. W., J. A. BROWSE, M. VOLOKITA, and S. G. BARTLETT: Spinach carbonic anhydrase primary structure deduced from the sequence of a cDNA clone. J. Biol. Chem. 265, 5414-5417 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 5414-5417
    • Fawcett, T.W.1    Browse, J.A.2    Volokita, M.3    Bartlett, S.G.4
  • 12
    • 0028169311 scopus 로고
    • Characterization of two membrane-associated β-glucosidases from maize (Zea mays L.) coleoptiles
    • FELDWISCH, J., A. VENTE, R. ZETTL, L. BAKO, N. CAMPOS, and K. PALME: Characterization of two membrane-associated β-glucosidases from maize (Zea mays L.) coleoptiles. Biochem. J. 302, 15-21 (1994).
    • (1994) Biochem. J. , vol.302 , pp. 15-21
    • Feldwisch, J.1    Vente, A.2    Zettl, R.3    Bako, L.4    Campos, N.5    Palme, K.6
  • 13
    • 0000506710 scopus 로고
    • Cross-linking of matrix polymers in the growing cell walls of angiosperms
    • FRY, S. C.: Cross-linking of matrix polymers in the growing cell walls of angiosperms. Annu. Rev. Plant Physiol. Plant Mol. Biol. 37, 165-186 (1986).
    • (1986) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.37 , pp. 165-186
    • Fry, S.C.1
  • 14
    • 0002071095 scopus 로고
    • In situ peptide mapping of proteins following polyacrylamide gel electrophoresis
    • WALKER, J. M. (ed.), Humana Press, Clifton, New Jersey
    • GOODERHAM, K.: In situ peptide mapping of proteins following polyacrylamide gel electrophoresis, pp. 193-202. In: WALKER, J. M. (ed.): Methods in Molecular Biology, Vol. 1: Proteins, Humana Press, Clifton, New Jersey (1984).
    • (1984) Methods in Molecular Biology, Vol. 1: Proteins , vol.1 , pp. 193-202
    • Gooderham, K.1
  • 15
    • 0021382845 scopus 로고
    • The interaction of proteins with hydroxyapatite. I. Role of protein charge and structure
    • GORBUNOFF, M. J.: The interaction of proteins with hydroxyapatite. I. Role of protein charge and structure. Anal. Biochem. 136, 425-432 (1984a).
    • (1984) Anal. Biochem. , vol.136 , pp. 425-432
    • Gorbunoff, M.J.1
  • 16
    • 0021380377 scopus 로고
    • The interaction of proteins with hydroxyapatite. II. Role of acidic and basic groups
    • -The interaction of proteins with hydroxyapatite. II. Role of acidic and basic groups. Anal. Biochem. 136, 433-439 (1984b).
    • (1984) Anal. Biochem. , vol.136 , pp. 433-439
  • 17
    • 0021382846 scopus 로고
    • The interaction of proteins with hydroxyapatite. III. Mechanism
    • GORBUNOFF, M. J. and S. N. TIMASHEFF: The interaction of proteins with hydroxyapatite. III. Mechanism. Anal. Biochem. 136, 440-445 (1984).
    • (1984) Anal. Biochem. , vol.136 , pp. 440-445
    • Gorbunoff, M.J.1    Timasheff, S.N.2
  • 18
    • 0000994164 scopus 로고
    • Characterization of a protein-kinase activity associated with phytochrome from etiolated oat (Avena sativa L.) seedlings
    • GRIMM, R., D. GAST, and W. RÜDIGER: Characterization of a protein-kinase activity associated with phytochrome from etiolated oat (Avena sativa L.) seedlings. Planta 178, 199-206 (1989).
    • (1989) Planta , vol.178 , pp. 199-206
    • Grimm, R.1    Gast, D.2    Rüdiger, W.3
  • 19
    • 0025698006 scopus 로고
    • 2+-dependent protein kinase from the green alga, Dunaliella salina
    • 2+-dependent protein kinase from the green alga, Dunaliella salina. Plant Physiol. 94, 143-150 (1990).
    • (1990) Plant Physiol. , vol.94 , pp. 143-150
    • Gou, Y.-L.1    Roux, S.J.2
  • 20
    • 0028307973 scopus 로고
    • The amino acid sequence previously attributed to a protein kinase or a TCP1 -related molecular chaperone and co-purified with phytochrome is a β-glucosidase
    • GUS-MAYER, S., H. BRUNNER, H. A. W. SCHNEIDER-POETSCH, F. LOTTSPEICH, C. ECKERSKORN, R. GRIMM, and W. RÜDIGER: The amino acid sequence previously attributed to a protein kinase or a TCP1 -related molecular chaperone and co-purified with phytochrome is a β-glucosidase. FEBS Lett. 347, 51-54 (1994),
    • (1994) FEBS Lett. , vol.347 , pp. 51-54
    • Gus-Mayer, S.1    Brunner, H.2    Schneider-Poetsch, H.A.W.3    Lottspeich, F.4    Eckerskorn, C.5    Grimm, R.6    Rüdiger, W.7
  • 21
    • 0000510324 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • EISENTHAL, R. and M. J. DANSON (eds.), IRL Press at Oxford University Press, Oxford, England
    • HENDERSON, P. J. F: Statistical analysis of enzyme kinetic data, pp. 277-316. In: EISENTHAL, R. and M. J. DANSON (eds.): Enzyme Assays: A Practical Approach, IRL Press at Oxford University Press, Oxford, England (1992).
    • (1992) Enzyme Assays: A Practical Approach , pp. 277-316
    • Henderson, P.J.F.1
  • 22
    • 0020573442 scopus 로고
    • Efficient transfer of proteins from acetic acid-urea and isoelectric-focusing gels to nitrocellulose membrane filters with retention of protein antigenicity
    • JOHNSON, T. K., K. C. L. YUEN, R. E. DENELL, and R. A. CONSIGLI: Efficient transfer of proteins from acetic acid-urea and isoelectric-focusing gels to nitrocellulose membrane filters with retention of protein antigenicity. Anal. Biochem. 133, 126-131 (1983).
    • (1983) Anal. Biochem. , vol.133 , pp. 126-131
    • Johnson, T.K.1    Yuen, K.C.L.2    Denell, R.E.3    Consigli, R.A.4
  • 23
    • 0344817973 scopus 로고    scopus 로고
    • Immunocytolocalization of cell wall peroxidase and other wall antigens from maize seedlings
    • KIM, S.-H., M. DAUWALDER, and S. J. ROUX Jr.: Immunocytolocalization of cell wall peroxidase and other wall antigens from maize seedlings. J. Plant Biol. 39, 99-105 (1996).
    • (1996) J. Plant Biol. , vol.39 , pp. 99-105
    • Kim, S.-H.1    Dauwalder, M.2    Roux S.J., Jr.3
  • 24
    • 0024787667 scopus 로고
    • Phytochrome induces changes in the immunodetectable level of a wall peroxidase that precedes growth changes in maize seedlings
    • KIM, S.-H., J. R. SHINKLE, and S. J. ROUX: Phytochrome induces changes in the immunodetectable level of a wall peroxidase that precedes growth changes in maize seedlings. Proc. Natl. Acad. Sci. USA 86, 9866-9870 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9866-9870
    • Kim, S.-H.1    Shinkle, J.R.2    Roux, S.J.3
  • 25
    • 0024274917 scopus 로고
    • Production and characterization of monoclonal antibodies to wall-localized peroxidases from corn seedlings
    • KIM, S.-H., M. E. TERRY, P. HOOPS, M. DAUWALDER, and S. J. ROUX: Production and characterization of monoclonal antibodies to wall-localized peroxidases from corn seedlings. Plant Physiol. 88, 1446-1453 (1988).
    • (1988) Plant Physiol. , vol.88 , pp. 1446-1453
    • Kim, S.-H.1    Terry, M.E.2    Hoops, P.3    Dauwalder, M.4    Roux, S.J.5
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • LAEMMLI, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685 (1970).
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 11544297023 scopus 로고
    • Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase
    • LAGRIMINI, L. M.: Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase. Plant Physiol. 96, 577-583 (1991).
    • (1991) Plant Physiol. , vol.96 , pp. 577-583
    • Lagrimini, L.M.1
  • 28
  • 30
    • 0000521648 scopus 로고
    • Unique properties of cell wall-associated β-glucosidases
    • NAGAHASHI, G., D. G. LASSITER, and D. L. PATTERSON: Unique properties of cell wall-associated β-glucosidases. Plant Sci. 81, 163-168 (1992).
    • (1992) Plant Sci. , vol.81 , pp. 163-168
    • Nagahashi, G.1    Lassiter, D.G.2    Patterson, D.L.3
  • 32
    • 0030792334 scopus 로고    scopus 로고
    • IAA breakdown and its effect of auxin-induced cell wall acidification in maize coleoptile segments
    • PETERS, W. S., C. LOMMEL, and H. FELLE: IAA breakdown and its effect of auxin-induced cell wall acidification in maize coleoptile segments. Physiol. Plant. 100, 415-422 (1997).
    • (1997) Physiol. Plant. , vol.100 , pp. 415-422
    • Peters, W.S.1    Lommel, C.2    Felle, H.3
  • 33
    • 0027692039 scopus 로고
    • Improved chromatographic purification of peroxidase and β-glucosidase from Hordeum vulgare seedlings
    • RESCIGNO, A., E. SANJUST, N. CURRELI, A. PADIGLIA, and G. FLORIS: Improved chromatographic purification of peroxidase and β-glucosidase from Hordeum vulgare seedlings. Prepar. Biochem. 23, 485-492 (1993).
    • (1993) Prepar. Biochem. , vol.23 , pp. 485-492
    • Rescigno, A.1    Sanjust, E.2    Curreli, N.3    Padiglia, A.4    Floris, G.5
  • 34
    • 84994999029 scopus 로고
    • Lupin peroxidases. I. Isolation and characterization of cell wall-bound isoperoxidase activity
    • ROS BARCELÓ, A., R. MUÑOZ, and F. SABATER: Lupin peroxidases. I. Isolation and characterization of cell wall-bound isoperoxidase activity. Physiol. Plant. 71, 448-454 (1987).
    • (1987) Physiol. Plant. , vol.71 , pp. 448-454
    • Ros Barceló, A.1    Muñoz, R.2    Sabater, F.3
  • 35
    • 0016824490 scopus 로고
    • The nature of experimental error in enzyme-kinetic measurements
    • STORER, A. C., M. G. DARLISON, and A. CORNISH-BOWDEN: The nature of experimental error in enzyme-kinetic measurements. Biochem. J. 151, 361-367 (1975).
    • (1975) Biochem. J. , vol.151 , pp. 361-367
    • Storer, A.C.1    Darlison, M.G.2    Cornish-Bowden, A.3
  • 36
    • 0030132753 scopus 로고    scopus 로고
    • Apoplastic pH in corn root gravitropism: A laser scanning confocal microscopy measurement
    • TAYLOR, D. P., J. SLATTERY, and A. C. LEOPOLD: Apoplastic pH in corn root gravitropism: A laser scanning confocal microscopy measurement. Physiol. Plant. 97, 35-38 (1996).
    • (1996) Physiol. Plant. , vol.97 , pp. 35-38
    • Taylor, D.P.1    Slattery, J.2    Leopold, A.C.3
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • TOWBIN, H., T. STAEHELIN, and J. GORDON: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354 (1979).
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


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