메뉴 건너뛰기




Volumn 50, Issue 3, 2002, Pages 199-206

Elicitation effects of chitin oligomers and chitosan sprayed on the leaves of cucumber (Cucumis sativus) and bean (Phaseolus vulgaris) plants

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; SPRAY; VEGETABLE;

EID: 0036385038     PISSN: 07929978     EISSN: None     Source Type: Journal    
DOI: 10.1092/HQRC-H136-PJBJ-R1R1     Document Type: Article
Times cited : (11)

References (34)
  • 1
    • 0014769211 scopus 로고
    • Temporal and hormonal control of β-1,3-glucans in Phaseolus vulgaris L.
    • Abeles, F.B., Forrence, L.E. 1979. Temporal and hormonal control of β-1,3-glucans in Phaseolus vulgaris L. Plant Physiol. 45: 395-400.
    • (1979) Plant Physiol. , vol.45 , pp. 395-400
    • Abeles, F.B.1    Forrence, L.E.2
  • 2
    • 0026692774 scopus 로고
    • A convenient assay for chitinase that uses partially N-acetylated chitosans as substrates
    • Aiba, S. 1992. A convenient assay for chitinase that uses partially N-acetylated chitosans as substrates. Carbohydr. Res. 230: 373-376.
    • (1992) Carbohydr. Res. , vol.230 , pp. 373-376
    • Aiba, S.1
  • 3
    • 0002261005 scopus 로고
    • The behaviour of chitin towards anhydrous hydrogen fluoride preparation of β-1,4-linked-2-acetamido-2-deoxy-D-glucopyranosyl oligosaccharides
    • Bosso, C., Defaye, J., Domard, A., Gadelle, A. 1986. The behaviour of chitin towards anhydrous hydrogen fluoride preparation of β-1,4-linked-2-acetamido-2-deoxy-D-glucopyranosyl oligosaccharides. Carbohydr. Res. 156: 57-68.
    • (1986) Carbohydr. Res. , vol.156 , pp. 57-68
    • Bosso, C.1    Defaye, J.2    Domard, A.3    Gadelle, A.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 78651153791 scopus 로고
    • Disc electrophoresis II. Method and application to human serum proteins
    • Davis, B.J. 1964. Disc electrophoresis II. Method and application to human serum proteins. Ann. New York Acad. Sci. 121: 404-427.
    • (1964) Ann. New York Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 6
    • 0028354159 scopus 로고
    • Elicitors of plant defense responses
    • Ebel, J., Casio, E.G. 1994. Elicitors of plant defense responses. Int. Rev. Cytol. 148: 1-36.
    • (1994) Int. Rev. Cytol. , vol.148 , pp. 1-36
    • Ebel, J.1    Casio, E.G.2
  • 7
    • 0000406646 scopus 로고
    • Antifungal activity of chitosan on two postharvest pathogens of strawberry fruits
    • El Ghaouth, A., Arul, J., Grenier, J., Asselin, A. 1992. Antifungal activity of chitosan on two postharvest pathogens of strawberry fruits. Phytopathology 82: 398-402.
    • (1992) Phytopathology , vol.82 , pp. 398-402
    • El Ghaouth, A.1    Arul, J.2    Grenier, J.3    Asselin, A.4
  • 8
    • 0028155916 scopus 로고
    • Effect of chitosan on cucumber plants: Suppression of Phytium aphanidermatum and induction of defense reactions
    • El Ghaouth, A., Arul, J., Grenier, J., Benhamou, N., Asselin, A., Belanger, R. 1994. Effect of chitosan on cucumber plants: suppression of Phytium aphanidermatum and induction of defense reactions. Phytopathology 84: 313-320.
    • (1994) Phytopathology , vol.84 , pp. 313-320
    • El Ghaouth, A.1    Arul, J.2    Grenier, J.3    Benhamou, N.4    Asselin, A.5    Belanger, R.6
  • 9
    • 0001390371 scopus 로고
    • Plant lectins: Molecular and biological aspects
    • Etzler, M.E. 1985. Plant lectins: molecular and biological aspects. Annu. Rev. Plant Physiol. 36: 209-234.
    • (1985) Annu. Rev. Plant Physiol. , vol.36 , pp. 209-234
    • Etzler, M.E.1
  • 10
    • 0000538103 scopus 로고
    • Specific perception of subnanomolar concentrations of chitin fragments by tomato cells: Induction of extracellular alkalisation, changes in protein phosphorylation, and establishment of a refractory state
    • Felix, G., Regenass, M., Boler, T. 1993. Specific perception of subnanomolar concentrations of chitin fragments by tomato cells: induction of extracellular alkalisation, changes in protein phosphorylation, and establishment of a refractory state. Plant J. 4: 307-316.
    • (1993) Plant J. , vol.4 , pp. 307-316
    • Felix, G.1    Regenass, M.2    Boler, T.3
  • 11
    • 12044255366 scopus 로고
    • Rapid accumulation of anionic peroxidases and phenolic chitosans in soybean cotyledon tissues following treatment with Phytophthora megasperma f. sp. glycinea wall glucan
    • Graham, M.Y., Graham, T.L. 1992. Rapid accumulation of anionic peroxidases and phenolic chitosans in soybean cotyledon tissues following treatment with Phytophthora megasperma f. sp. glycinea wall glucan. Plant Physiol. 97: 1445-1455.
    • (1992) Plant Physiol. , vol.97 , pp. 1445-1455
    • Graham, M.Y.1    Graham, T.L.2
  • 12
    • 0001361165 scopus 로고
    • Some pathogenesis-related proteins are chitosanases with lytic activity against fungal spores
    • Grenier, J., Asselin, A. 1990. Some pathogenesis-related proteins are chitosanases with lytic activity against fungal spores. Molecular Plant Mycology Interaction 6: 401-407.
    • (1990) Molecular Plant Mycology Interaction , vol.6 , pp. 401-407
    • Grenier, J.1    Asselin, A.2
  • 13
    • 0000568294 scopus 로고
    • Effect of chitosan, pectic acid, lysozyme and chitinase on the growth of several phytopathogens
    • Hirano, S., Nagao, N. 1989. Effect of chitosan, pectic acid, lysozyme and chitinase on the growth of several phytopathogens. Agric. Biol. Chem. 53: 3065-3066.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 3065-3066
    • Hirano, S.1    Nagao, N.2
  • 14
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T., Yagishita, K. 1971. A simple activity measurement of lysozyme. Agric. Biol. Chem. 35: 1154-1156.
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 15
    • 0031171845 scopus 로고    scopus 로고
    • Elicitor actions of N-acetylchitooligosaccharides and laminarin-oligosaccharides for chitinase and L-phenylalanine ammonia-lyase induction in rice suspension culture
    • Inui, H., Yamaguchi, Y., Hirano, S. 1997. Elicitor actions of N-acetylchitooligosaccharides and laminarin-oligosaccharides for chitinase and L-phenylalanine ammonia-lyase induction in rice suspension culture. Biosci. Biotech. Biochem. 61: 975-978.
    • (1997) Biosci. Biotech. Biochem. , vol.61 , pp. 975-978
    • Inui, H.1    Yamaguchi, Y.2    Hirano, S.3
  • 16
    • 0029411286 scopus 로고
    • Purification and characterization of an acidic β-1,3-glucanase from cucumber and its relationship to systemic disease resistance induced by Colletotrichum lagenarium and Tobacco Necrosis Virus
    • Ji, C., Kue, J. 1995. Purification and characterization of an acidic β-1,3-glucanase from cucumber and its relationship to systemic disease resistance induced by Colletotrichum lagenarium and Tobacco Necrosis Virus. Mol. Pl.-Mic. Int. 8: 889-905.
    • (1995) Mol. Pl.-Mic. Int. , vol.8 , pp. 889-905
    • Ji, C.1    Kue, J.2
  • 17
    • 0020727065 scopus 로고
    • Lipid deterioration initiated by phagocytic cells in muscle foods: β-carotene destruction by a myeloperoxidase-hydrogen peroxide-halide system
    • Kanner, J., Kinsella, J.E. 1983. Lipid deterioration initiated by phagocytic cells in muscle foods: β-carotene destruction by a myeloperoxidase-hydrogen peroxide-halide system. J. Agric. Food Chem. 31: 370-376.
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 370-376
    • Kanner, J.1    Kinsella, J.E.2
  • 18
    • 0001516391 scopus 로고
    • The degree of chitosanization and N-acetylation of chitosan determine its ability to elicit callose formation in suspension cells and protoplasts of Catharanthus roseus
    • Kauss, H., Jeblick, W., Domard, A. 1989. The degree of chitosanization and N-acetylation of chitosan determine its ability to elicit callose formation in suspension cells and protoplasts of Catharanthus roseus. Planta 178: 385-392.
    • (1989) Planta , vol.178 , pp. 385-392
    • Kauss, H.1    Jeblick, W.2    Domard, A.3
  • 19
    • 0000764787 scopus 로고    scopus 로고
    • Development of integrated pest management techniques using biomass for organic farming (I). Suppression of late blight and fusarium wilt of tomato by chitosan
    • Keun Oh, S., Choi, D., Hun Yu, S. 1998. Development of integrated pest management techniques using biomass for organic farming (I). Suppression of late blight and fusarium wilt of tomato by chitosan. Korean J. Plant Pathol. 14: 278-285.
    • (1998) Korean J. Plant Pathol. , vol.14 , pp. 278-285
    • Keun Oh, S.1    Choi, D.2    Hun Yu, S.3
  • 20
    • 0002690521 scopus 로고
    • Isolation from Rubus cell-suspension cultures of a lectin specific for glucosamine oligomers
    • Lienart, Y., Gautier, C., Domard, A. 1991. Isolation from Rubus cell-suspension cultures of a lectin specific for glucosamine oligomers. Planta 184: 8-13.
    • (1991) Planta , vol.184 , pp. 8-13
    • Lienart, Y.1    Gautier, C.2    Domard, A.3
  • 21
    • 0030861162 scopus 로고    scopus 로고
    • The possible involvement of peroxidase in resistance to Botrytis cinerea in heat-treated tomato fruit
    • Lurie, S., Fallik, E., Handros, A., Shapira, R. 1997. The possible involvement of peroxidase in resistance to Botrytis cinerea in heat-treated tomato fruit. Phys. Mol. Plant Path. 50: 141-149.
    • (1997) Phys. Mol. Plant Path. , vol.50 , pp. 141-149
    • Lurie, S.1    Fallik, E.2    Handros, A.3    Shapira, R.4
  • 22
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves
    • Mauch, F., Staehelin, A., 1989. Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant Cell 1: 447-457.
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Staehelin, A.2
  • 23
    • 0027551631 scopus 로고
    • Preparation and crystallization of D-glucosamine oligosaccharides with DP 6-8
    • Muraki, F., Yaku, F., Kojima, H. 1993. Preparation and crystallization of D-glucosamine oligosaccharides with DP 6-8. Carbohydr. Res. 239: 227-237.
    • (1993) Carbohydr. Res. , vol.239 , pp. 227-237
    • Muraki, F.1    Yaku, F.2    Kojima, H.3
  • 24
    • 0000674033 scopus 로고
    • A photometric adaptation of the Somogyi method for the determination of glucose
    • Nelson, N. 1944. A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153: 375-380.
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, N.1
  • 25
    • 0024746614 scopus 로고
    • Direct detection of β-1,3-glucanase isozymes on polyacrylamide electrophoresis and isoelectrofocusing gels
    • Pan, S.Q., Ye, X.S., Kuc, J. 1989. Direct detection of β-1,3-glucanase isozymes on polyacrylamide electrophoresis and isoelectrofocusing gels. Anal. Biochem. 182: 136-140.
    • (1989) Anal. Biochem. , vol.182 , pp. 136-140
    • Pan, S.Q.1    Ye, X.S.2    Kuc, J.3
  • 26
    • 0001926497 scopus 로고
    • Induction of antiviral resistance in plants by chitosan
    • Pospieszny, H., Churkov, S., Atabekov, J. 1991. Induction of antiviral resistance in plants by chitosan. Plant Sci. 79: 63-68.
    • (1991) Plant Sci. , vol.79 , pp. 63-68
    • Pospieszny, H.1    Churkov, S.2    Atabekov, J.3
  • 27
    • 0023667844 scopus 로고
    • Chitin oligosaccharides as elicitors of chitinase activity in melon plants
    • Roby, D., Gadelle, A., Toppan, A. 1987. Chitin oligosaccharides as elicitors of chitinase activity in melon plants. Biochem. Biophys. Res. Commun. 143: 885-892.
    • (1987) Biochem. Biophys. Res. Commun. , vol.143 , pp. 885-892
    • Roby, D.1    Gadelle, A.2    Toppan, A.3
  • 28
    • 0027326649 scopus 로고
    • Identification of a novel high-affinity-binding site for N-acetylchitooligosaccharide elicitor in the membrane fraction of suspension cultured rice cells
    • Shibuya, N., Kaku, H., Kuchitsu, K., Maliarik, M.J. 1993. Identification of a novel high-affinity-binding site for N-acetylchitooligosaccharide elicitor in the membrane fraction of suspension cultured rice cells. FEBS Lett. 329: 75-78.
    • (1993) FEBS Lett. , vol.329 , pp. 75-78
    • Shibuya, N.1    Kaku, H.2    Kuchitsu, K.3    Maliarik, M.J.4
  • 29
    • 0029807346 scopus 로고    scopus 로고
    • Localisation and binding characteristics of a high affinity binding site for N-acetylchitooligosaccharide elicitor in the plasma membrane from suspension-cultured rice cells suggest a role as a receptor for the elicitor signal at the cell surface
    • Shibuya, N., Kaku, H., Kuchitsu, K., Maliarik, M.J. 1996. Localisation and binding characteristics of a high affinity binding site for N-acetylchitooligosaccharide elicitor in the plasma membrane from suspension-cultured rice cells suggest a role as a receptor for the elicitor signal at the cell surface. Plant Cell Physiol. 37: 894-898.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 894-898
    • Shibuya, N.1    Kaku, H.2    Kuchitsu, K.3    Maliarik, M.J.4
  • 30
    • 0028360825 scopus 로고
    • A method for activity staining of peroxidase and β-1,3-glucanase isozymes in polyacrylamide electrophoresis gels
    • Shimoni, M. 1994. A method for activity staining of peroxidase and β-1,3-glucanase isozymes in polyacrylamide electrophoresis gels. Anal. Biochem. 220: 36-38.
    • (1994) Anal. Biochem. , vol.220 , pp. 36-38
    • Shimoni, M.1
  • 31
    • 0001067592 scopus 로고    scopus 로고
    • Chitosan: Mechanism of action and ways of using as ecologically safe means in enhancement of plant disease resistance
    • Tiuterev, S., Yakubchik, M., Tarlakovsky, S., Popova, E., Vytsky, V., Dorofeyeva, T. 1996. Chitosan: mechanism of action and ways of using as ecologically safe means in enhancement of plant disease resistance. Arch. Phytopath. Pflanz. 30: 323-332.
    • (1996) Arch. Phytopath. Pflanz. , vol.30 , pp. 323-332
    • Tiuterev, S.1    Yakubchik, M.2    Tarlakovsky, S.3    Popova, E.4    Vytsky, V.5    Dorofeyeva, T.6
  • 32
    • 0024669485 scopus 로고
    • Detection of chitinase activity after polyacrylamide gel electrophoresis
    • Trudel, J., Asselin, A. 1989. Detection of chitinase activity after polyacrylamide gel electrophoresis. Anal. Biochem. 178: 362-366.
    • (1989) Anal. Biochem. , vol.178 , pp. 362-366
    • Trudel, J.1    Asselin, A.2
  • 33
    • 0001007252 scopus 로고    scopus 로고
    • Comparison of the ability of partially N-acetylated chitosans and oligosaccharides to elicit resistence in wheat leaves
    • Vander, P., Kjell, M.V., Domard, A., El-Gueddari, N.E., Moerschbacher, B.M. 1998. Comperison of the ability of partially N-acetylated chitosans and oligosaccharides to elicit resistence in wheat leaves. Plant Physiol. 118: 1353-1359.
    • (1998) Plant Physiol. , vol.118 , pp. 1353-1359
    • Vander, P.1    Kjell, M.V.2    Domard, A.3    El-Gueddari, N.E.4    Moerschbacher, B.M.5
  • 34
    • 0000956263 scopus 로고
    • Induction of phytoalexin formation in suspension-cultured rice cells by N-acetyl-chitooligosaccharides
    • Yamada, T., Shibuya, N., Kodoma, O., Akatsuka, T. 1993. Induction of phytoalexin formation in suspension-cultured rice cells by N-acetyl-chitooligosaccharides. Biosci. Biotech. Biochem. 57: 405-409.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 405-409
    • Yamada, T.1    Shibuya, N.2    Kodoma, O.3    Akatsuka, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.