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Volumn 80, Issue 2, 2003, Pages 144-147

Aryl-glycosidase activities in germinating maize

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS;

EID: 0037341405     PISSN: 00090352     EISSN: None     Source Type: Journal    
DOI: 10.1094/CCHEM.2003.80.2.144     Document Type: Article
Times cited : (10)

References (30)
  • 1
    • 0031025401 scopus 로고    scopus 로고
    • Structure, hormonal regulation, and chromosomal location of genes encoding barley (1→4)-β-xylan endohydrolases
    • Banik, M., Li, C.-D., Langridge, P., and Fincher, G. B. 1997. Structure, hormonal regulation, and chromosomal location of genes encoding barley (1→4)-β-xylan endohydrolases. Mol. Gen. Genet. 253:599-608.
    • (1997) Mol. Gen. Genet. , vol.253 , pp. 599-608
    • Banik, M.1    Li, C.-D.2    Langridge, P.3    Fincher, G.B.4
  • 2
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey, M. J., Biely, P., and Poutanen, K. 1992. Interlaboratory testing of methods for assay of xylanase activity. J. Biotechnol. 23:257-270.
    • (1992) J. Biotechnol. , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 3
    • 0021936912 scopus 로고
    • Sensitive detection of endo-1,4-β-glucanases and endo-1,4-β-xylanases in gels
    • Biely, P., Markovic, O., and Mislovicova, D. 1985. Sensitive detection of endo-1,4-β-glucanases and endo-1,4-β-xylanases in gels. Anal. Biochem. 144:147-151.
    • (1985) Anal. Biochem. , vol.144 , pp. 147-151
    • Biely, P.1    Markovic, O.2    Mislovicova, D.3
  • 4
    • 0002505638 scopus 로고
    • Identification and mode of action of endo-(1-4)-β-xylanases
    • J. Visser, G. Beldman, M. A. Kuster-van Someren, and A. G. J. Voragen, eds. Elsevier Science Publishers: Amsterdam
    • Biely, P., Vrsanska, M., and Kucar, S. 1992. Identification and mode of action of endo-(1-4)-β-xylanases. Pages 81-95 in: Xylan and Xylanases. J. Visser, G. Beldman, M. A. Kuster-van Someren, and A. G. J. Voragen, eds. Elsevier Science Publishers: Amsterdam.
    • (1992) Xylan and Xylanases , pp. 81-95
    • Biely, P.1    Vrsanska, M.2    Kucar, S.3
  • 5
    • 0034669364 scopus 로고    scopus 로고
    • A chromogenic substrate for a β-xylosidase-coupled assay of α-glucuronidase
    • Biely, P., Hirsch, J., la Grange, D. C., van Zyl, W. H., and Prior, B. A. 2000. A chromogenic substrate for a β-xylosidase-coupled assay of α-glucuronidase. Anal. Biochem. 286:289-294.
    • (2000) Anal. Biochem. , vol.286 , pp. 289-294
    • Biely, P.1    Hirsch, J.2    La Grange, D.C.3    Van Zyl, W.H.4    Prior, B.A.5
  • 6
    • 0012041350 scopus 로고    scopus 로고
    • The predominant protein on the surface of maize pollen is an endoxylanase synthesized by a tapetum mRNA with a long 5′ leader
    • Bih, F. Y., Wu, S. S. H., Ratnayake, C., Walling, L. L., Nothnagel, E. A., and Huang, A. H. C. 1999. The predominant protein on the surface of maize pollen is an endoxylanase synthesized by a tapetum mRNA with a long 5′ leader. J. Biol. Chem. 274:22884-22894.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22884-22894
    • Bih, F.Y.1    Wu, S.S.H.2    Ratnayake, C.3    Walling, L.L.4    Nothnagel, E.A.5    Huang, A.H.C.6
  • 7
    • 0019217328 scopus 로고
    • N-(1-Naphthyl)ethylenediamine dihydrochloride as a new reagent for nanomole quantification of sugars on thin-layer plates by a mathematical calibration process
    • Bounias, M. 1980. N-(1-Naphthyl)ethylenediamine dihydrochloride as a new reagent for nanomole quantification of sugars on thin-layer plates by a mathematical calibration process. Anal. Biochem. 106:291-295.
    • (1980) Anal. Biochem. , vol.106 , pp. 291-295
    • Bounias, M.1
  • 8
    • 0000014240 scopus 로고
    • Gibberellic-acid-induced synthesis and release of cell-wall-degrading endoxylanase by isolated aleurone layers of barley
    • Dashek, W. V., and Chrispeels, M. J. 1977. Gibberellic-acid-induced synthesis and release of cell-wall-degrading endoxylanase by isolated aleurone layers of barley. Planta 134:251-256.
    • (1977) Planta , vol.134 , pp. 251-256
    • Dashek, W.V.1    Chrispeels, M.J.2
  • 9
    • 0000860075 scopus 로고
    • Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains
    • W. R. Briggs, R. L. Jones, and V. Walbot, eds. Annual Reviews, Palo Alto, CA
    • Fincher, G. B. 1989. Molecular and cellular biology associated with endosperm mobilization in germinating cereal grains. Pages 305-346 in: Ann. Rev. Plant Physiol. Plant Mol. Biol. 40. W. R. Briggs, R. L. Jones, and V. Walbot, eds. Annual Reviews, Palo Alto, CA.
    • (1989) Ann. Rev. Plant Physiol. Plant Mol. Biol. , vol.40 , pp. 305-346
    • Fincher, G.B.1
  • 10
    • 0012394141 scopus 로고
    • Some chemical and morphological changes induced by gibberellic acid in embryo-free wheat germ
    • Fincher, G. B., and Stone, B. A. 1974. Some chemical and morphological changes induced by gibberellic acid in embryo-free wheat germ. Aust. J. Plant Physiol. 1:297-311.
    • (1974) Aust. J. Plant Physiol. , vol.1 , pp. 297-311
    • Fincher, G.B.1    Stone, B.A.2
  • 11
    • 0022954033 scopus 로고
    • Cereal walls and their components in cereal grain technology
    • Y. Pomeranz, ed. Am. Assoc. Cereal Chem.: St. Paul, MN
    • Fincher, G. B., and Stone, B. A. 1986. Cereal walls and their components in cereal grain technology. Pages 207-295 in: Advances in Cereal Science and Technology, Vol. 8. Y. Pomeranz, ed. Am. Assoc. Cereal Chem.: St. Paul, MN.
    • (1986) Advances in Cereal Science and Technology , vol.8 , pp. 207-295
    • Fincher, G.B.1    Stone, B.A.2
  • 12
    • 0017400203 scopus 로고
    • Studies on xylan degrading enzymes. 1. Purification and characterization of endo-1,4-β-xylanase from Aspergillus niger str. 14
    • Gorbacheva, I. V., and Rodionova, N. A. 1977. Studies on xylan degrading enzymes. 1. Purification and characterization of endo-1,4-β-xylanase from Aspergillus niger str. 14. Biochim. Biophys. Acta 484:79-93.
    • (1977) Biochim. Biophys. Acta , vol.484 , pp. 79-93
    • Gorbacheva, I.V.1    Rodionova, N.A.2
  • 13
    • 0000235162 scopus 로고    scopus 로고
    • Extraction and characterization of hemicellulose from the corn fiber produced by corn wet-milling processes
    • Hespell, R. B. 1998. Extraction and characterization of hemicellulose from the corn fiber produced by corn wet-milling processes. J. Agric. Food Chem. 46:2615-2619.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 2615-2619
    • Hespell, R.B.1
  • 14
    • 0002782296 scopus 로고    scopus 로고
    • Hydrolysis by commercial enzyme mixtures of AFEX-treated corn fiber and isolated xylans
    • Hespell, R. B., O'Bryan, P. J., Moniruzzaman, M., and Bothast, R. J. 1997. Hydrolysis by commercial enzyme mixtures of AFEX-treated corn fiber and isolated xylans. Appl. Biochem. Biotechnol. 62:87-97.
    • (1997) Appl. Biochem. Biotechnol. , vol.62 , pp. 87-97
    • Hespell, R.B.1    O'Bryan, P.J.2    Moniruzzaman, M.3    Bothast, R.J.4
  • 15
    • 37049155119 scopus 로고
    • Quantitative analysis of mixtures of sugars by the method of partition chromatography. V Improved methods for the separation and detection of their methylated derivatives on the paper chromatogram
    • Hough, L., Jones, J. K. N., and Wadman, W. H. 1950. Quantitative analysis of mixtures of sugars by the method of partition chromatography. V Improved methods for the separation and detection of their methylated derivatives on the paper chromatogram. J. Chem. Soc. 1702-1706.
    • (1950) J. Chem. Soc. , pp. 1702-1706
    • Hough, L.1    Jones, J.K.N.2    Wadman, W.H.3
  • 16
    • 0030798415 scopus 로고    scopus 로고
    • Regulation of cell wall glucanase activities by non-enzymic proteins in maize coleoptiles
    • Inouhe, M., and Nevins, D. 1997. Regulation of cell wall glucanase activities by non-enzymic proteins in maize coleoptiles. Int. J. Biol. Macromol. 21:15-20.
    • (1997) Int. J. Biol. Macromol. , vol.21 , pp. 15-20
    • Inouhe, M.1    Nevins, D.2
  • 17
    • 0031821511 scopus 로고    scopus 로고
    • Changes in the activities and polypeptide levels of exo- and endoglucanases in cell walls during developmental growth of Zea mays coleoptiles
    • Inouhe, M., and Nevins, D. J. 1998. Changes in the activities and polypeptide levels of exo- and endoglucanases in cell walls during developmental growth of Zea mays coleoptiles. Plant Cell Physiol. 39:762-768.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 762-768
    • Inouhe, M.1    Nevins, D.J.2
  • 18
    • 0032918458 scopus 로고    scopus 로고
    • Polypeptide characteristics and immunological properties of exo- and endoglucanases purified from maize coleoptile cell walls
    • Inouhe, M., Hayashi, K., and Nevins, D. J. 1999. Polypeptide characteristics and immunological properties of exo- and endoglucanases purified from maize coleoptile cell walls. J. Plant Physiol. 154:334-340.
    • (1999) J. Plant Physiol. , vol.154 , pp. 334-340
    • Inouhe, M.1    Hayashi, K.2    Nevins, D.J.3
  • 19
    • 0034038146 scopus 로고    scopus 로고
    • Cell wall autolytic activities and distribution of cell wall glucanases in Zea mays L. seedlings
    • Inouhe, M., Inada, G., Thomas, B. R., and Nevins, D. J. 2000. Cell wall autolytic activities and distribution of cell wall glucanases in Zea mays L. seedlings. Int. J. Biol. Macromol. 27:151-156.
    • (2000) Int. J. Biol. Macromol. , vol.27 , pp. 151-156
    • Inouhe, M.1    Inada, G.2    Thomas, B.R.3    Nevins, D.J.4
  • 20
    • 0002357090 scopus 로고
    • Cereal arabinoxylans: Advances in structure and physicochemical properties
    • Izydorczyk, M. S., and Biliaderis, C. G. 1995. Cereal arabinoxylans: Advances in structure and physicochemical properties. Carbohydr. Polym. 28:33-48.
    • (1995) Carbohydr. Polym. , vol.28 , pp. 33-48
    • Izydorczyk, M.S.1    Biliaderis, C.G.2
  • 21
    • 0022998285 scopus 로고
    • Color variants of Aureobasidium pullulans overproduce xylanase with extremely high specific activity
    • Leathers, T. D. 1986. Color variants of Aureobasidium pullulans overproduce xylanase with extremely high specific activity. Appl. Environ. Microbiol. 52:1026-1030.
    • (1986) Appl. Environ. Microbiol. , vol.52 , pp. 1026-1030
    • Leathers, T.D.1
  • 22
    • 0000993797 scopus 로고    scopus 로고
    • Saccharification of corn fiber using enzymes from Aureobasidium sp. strain NRRL Y-2311-1
    • Leathers, T. D., and Gupta, S. C. 1996. Saccharification of corn fiber using enzymes from Aureobasidium sp. strain NRRL Y-2311-1. Appl. Biochem. Biotechnol. 59:337-347.
    • (1996) Appl. Biochem. Biotechnol. , vol.59 , pp. 337-347
    • Leathers, T.D.1    Gupta, S.C.2
  • 23
    • 33747333106 scopus 로고
    • Use of dintrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dintrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 24
    • 84980121850 scopus 로고
    • Enzymic degradation of cereal hemicelluloses. II. Pattern of pentosan degradation
    • Preece, I. A., and MacDougall, M. 1958. Enzymic degradation of cereal hemicelluloses. II. Pattern of pentosan degradation. J. Inst. Brew. 64:489-500.
    • (1958) J. Inst. Brew. , vol.64 , pp. 489-500
    • Preece, I.A.1    MacDougall, M.2
  • 25
    • 0006398463 scopus 로고    scopus 로고
    • Enzymology of xylan degradation
    • ACS Symposium Series 723. S. H. Imam, R. V. Greene, and B. R. Zaidi, eds. Am. Chem. Soc.: Washington, DC
    • Saha, B. C., and Bothast, R. J. 1999. Enzymology of xylan degradation. Pages 167-194 in: Biopolymers: Utilizing Nature's Advanced Materials. ACS Symposium Series 723. S. H. Imam, R. V. Greene, and B. R. Zaidi, eds. Am. Chem. Soc.: Washington, DC.
    • (1999) Biopolymers: Utilizing Nature's Advanced Materials , pp. 167-194
    • Saha, B.C.1    Bothast, R.J.2
  • 28
    • 0012455633 scopus 로고
    • Hemicelluloses of the cementing layers and of some cell walls of the corn kernel
    • Seckinger, H. L., Wolf, M. J., and MacMasters, J. J. 1960. Hemicelluloses of the cementing layers and of some cell walls of the corn kernel. Cereal Chem. 38:121-128.
    • (1960) Cereal Chem. , vol.38 , pp. 121-128
    • Seckinger, H.L.1    Wolf, M.J.2    MacMasters, J.J.3
  • 29
    • 0024310205 scopus 로고
    • Purification and characterization of three (1→4)-β-D-xylan endohydrolases from germinated barley
    • Slade, A. M., Hoj, P. B., Morrice, N. A., and Fincher, G. B. 1989. Purification and characterization of three (1→4)-β-D-xylan endohydrolases from germinated barley. Eur. J. Biochem. 185:533-539.
    • (1989) Eur. J. Biochem. , vol.185 , pp. 533-539
    • Slade, A.M.1    Hoj, P.B.2    Morrice, N.A.3    Fincher, G.B.4
  • 30
    • 0001033505 scopus 로고
    • Production of cell wall hydrolyzing enzymes by barley aleurone layers in response to gibberellic acid
    • Taiz, L., and Honigman, W. A. 1976. Production of cell wall hydrolyzing enzymes by barley aleurone layers in response to gibberellic acid. Plant Physiol. 58:380-386.
    • (1976) Plant Physiol. , vol.58 , pp. 380-386
    • Taiz, L.1    Honigman, W.A.2


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