메뉴 건너뛰기




Volumn 89, Issue 10, 1999, Pages 902-907

A corn trypsin inhibitor with antifungal activity inhibits Aspergillus flavus α-amylase

Author keywords

Antifungal protein; Maize

Indexed keywords

AMYLASE; CULTURE MEDIUM; ENZYME INHIBITOR; GELATIN; GLUCOSE; MAIZE; PLANT DISEASE CONTROL; TRYPSIN;

EID: 0032868720     PISSN: 0031949X     EISSN: None     Source Type: Journal    
DOI: 10.1094/PHYTO.1999.89.10.902     Document Type: Article
Times cited : (86)

References (37)
  • 1
    • 0000595393 scopus 로고
    • Incorporation of labelled compounds into aflatoxin
    • Adye, J., and Mateles, R. I. 1964. Incorporation of labelled compounds into aflatoxin. Biochim. Biophys. Acta 86:418-420.
    • (1964) Biochim. Biophys. Acta , vol.86 , pp. 418-420
    • Adye, J.1    Mateles, R.I.2
  • 3
    • 84986519261 scopus 로고
    • Purification and characterization of an α-amylase inhibitor from maize (Zea maize)
    • Blanco-Labra, A., and Iturbe-Chinas, F. A. 1981. Purification and characterization of an α-amylase inhibitor from maize (Zea maize). J. Food Biochem. 5:1-17.
    • (1981) J. Food Biochem. , vol.5 , pp. 1-17
    • Blanco-Labra, A.1    Iturbe-Chinas, F.A.2
  • 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
    • 0001260377 scopus 로고
    • Plant proteinase inhibitors: Mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exiqua
    • Broadway, R. M., and Duffey, S. S. 1986. Plant proteinase inhibitors: Mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exiqua. J. Insect Physiol. 32:827-833.
    • (1986) J. Insect Physiol. , vol.32 , pp. 827-833
    • Broadway, R.M.1    Duffey, S.S.2
  • 6
    • 0032904779 scopus 로고    scopus 로고
    • Advances in the development of host resistance in corn to aflatoxin contamination by Aspergillus flavus
    • Brown, R. L., Chen, Z.-Y., Cleveland, T. E., and Russin, J. S. 1999. Advances in the development of host resistance in corn to aflatoxin contamination by Aspergillus flavus. Phytopathology 89:113-117.
    • (1999) Phytopathology , vol.89 , pp. 113-117
    • Brown, R.L.1    Chen, Z.-Y.2    Cleveland, T.E.3    Russin, J.S.4
  • 8
    • 0028855450 scopus 로고
    • Determination of resistance to aflatoxin production in maize kernels and detection of fungal colonization using an Aspergillus flavus transformant expressing Esrherichia roll β-glucuronidase
    • Brown, R. L., Cleveland, T. E., Payne, G. A., Woloshuk, C. P., Campbell, K. W., and White, D. G. 1995. Determination of resistance to aflatoxin production in maize kernels and detection of fungal colonization using an Aspergillus flavus transformant expressing Esrherichia roll β-glucuronidase. Phytopathology 85:983-989.
    • (1995) Phytopathology , vol.85 , pp. 983-989
    • Brown, R.L.1    Cleveland, T.E.2    Payne, G.A.3    Woloshuk, C.P.4    Campbell, K.W.5    White, D.G.6
  • 9
  • 10
    • 0033033179 scopus 로고    scopus 로고
    • Inhibition of plant-pathogenic fungi by a corn trypsin inhibitor over-expressed in Esrherichia coli
    • Chen, Z.-Y., Brown, R. L., Lax, A. R., Cleveland, T. E., and Russin, J. S. 1999. Inhibition of plant-pathogenic fungi by a corn trypsin inhibitor over-expressed in Esrherichia coli. Appl. Environ. Microbiol. 65:1320-1324.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1320-1324
    • Chen, Z.-Y.1    Brown, R.L.2    Lax, A.R.3    Cleveland, T.E.4    Russin, J.S.5
  • 11
    • 0031941096 scopus 로고    scopus 로고
    • Resistance to Aspergillus flavus in corn kernels is associated with a 14-kDa protein
    • Chen, Z.-Y., Brown, R. L., Lax, A. R., Guo, B. Z., Cleveland, T. E., and Russin, J. S. 1998. Resistance to Aspergillus flavus in corn kernels is associated with a 14-kDa protein. Phytopathology 88:276-281.
    • (1998) Phytopathology , vol.88 , pp. 276-281
    • Chen, Z.-Y.1    Brown, R.L.2    Lax, A.R.3    Guo, B.Z.4    Cleveland, T.E.5    Russin, J.S.6
  • 12
    • 25344464288 scopus 로고    scopus 로고
    • A corn trypsin inhibitor with antifungal activity and associated with host resistance to aflatoxin elaboration inhibits Aspergillus flavus alpha-amylase production
    • Chen, Z.-Y., Brown, R. L., Russin, J. S., Lax, A. R., and Cleveland, T. E. 1998. A corn trypsin inhibitor with antifungal activity and associated with host resistance to aflatoxin elaboration inhibits Aspergillus flavus alpha-amylase production. (Abstr.) Phytopathology 88(suppl.):S16.
    • (1998) Phytopathology , vol.88 , Issue.SUPPL.
    • Chen, Z.-Y.1    Brown, R.L.2    Russin, J.S.3    Lax, A.R.4    Cleveland, T.E.5
  • 13
    • 0001698624 scopus 로고
    • Virulence and cultural characteristics of two Aspergillus flavus strains pathogenic on cotton
    • Cotty, P. J. 1989. Virulence and cultural characteristics of two Aspergillus flavus strains pathogenic on cotton. Phytopathology 79:808-814.
    • (1989) Phytopathology , vol.79 , pp. 808-814
    • Cotty, P.J.1
  • 14
    • 0030918037 scopus 로고    scopus 로고
    • Multidrug resistance in Aspergillus nidulans involves novel ATP-binding cassette transporters
    • Del Sorbo, G., Andrade, A. C., Van Nistelrooy, J. G. M., Balzi, E., and De Waard, M. A. 1997. Multidrug resistance in Aspergillus nidulans involves novel ATP-binding cassette transporters. Mol. Gen. Genet. 254:417-426.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 417-426
    • Del Sorbo, G.1    Andrade, A.C.2    Van Nistelrooy, J.G.M.3    Balzi, E.4    De Waard, M.A.5
  • 15
    • 0030781183 scopus 로고    scopus 로고
    • Significance of ABC transporters in fungicide sensitivity and resistance
    • De Waard, M. A. 1997. Significance of ABC transporters in fungicide sensitivity and resistance. Pestic. Sci. 51:271-275.
    • (1997) Pestic. Sci. , vol.51 , pp. 271-275
    • De Waard, M.A.1
  • 17
    • 0030088668 scopus 로고    scopus 로고
    • Resistance to aflatoxin contamination in corn as influenced by relative humidity and kernel germination
    • Guo, B. Z., Russin, J. S., Cleveland, T. E., Brown, R. L., and Widstrom, N. W. 1996. Resistance to aflatoxin contamination in corn as influenced by relative humidity and kernel germination. J. Food Prot. 59:276-281.
    • (1996) J. Food Prot. , vol.59 , pp. 276-281
    • Guo, B.Z.1    Russin, J.S.2    Cleveland, T.E.3    Brown, R.L.4    Widstrom, N.W.5
  • 19
    • 0019129293 scopus 로고
    • Hageman factor fragment inhibitor in corn seeds: Purification and characterization
    • Hojima, Y., Pierce, J. V., and Pisano, J. J. 1980. Hageman factor fragment inhibitor in corn seeds: Purification and characterization. Thromb. Res. 20:149-162.
    • (1980) Thromb. Res. , vol.20 , pp. 149-162
    • Hojima, Y.1    Pierce, J.V.2    Pisano, J.J.3
  • 20
    • 0026598850 scopus 로고
    • Isolation and characterization of a 22 kDa protein with antifungal properties from maize seeds
    • Huynh, Q. K., Borgmeyer, J. R., and Zobel, J. F. 1992. Isolation and characterization of a 22 kDa protein with antifungal properties from maize seeds. Biochem. Biophys. Res. Commun. 182:1-5.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1-5
    • Huynh, Q.K.1    Borgmeyer, J.R.2    Zobel, J.F.3
  • 22
    • 0027949779 scopus 로고
    • Antifungal proteins from sorghum endosperm and their effects on fungal mycelium
    • Kumari, R. S., Chandrashekar, A., and Shetty, H. S. 1994. Antifungal proteins from sorghum endosperm and their effects on fungal mycelium. J. Sci. Food Agric. 66:121-127.
    • (1994) J. Sci. Food Agric. , vol.66 , pp. 121-127
    • Kumari, R.S.1    Chandrashekar, A.2    Shetty, H.S.3
  • 23
    • 0022637635 scopus 로고
    • Isolation and characterization of an amylase inhibitor from sorghum seeds, specific for human enzymes
    • Kutty, A. V. M., and Pattabiraman, T. N. 1986. Isolation and characterization of an amylase inhibitor from sorghum seeds, specific for human enzymes. J. Agric. Food Chem. 34:552-557.
    • (1986) J. Agric. Food Chem. , vol.34 , pp. 552-557
    • Kutty, A.V.M.1    Pattabiraman, T.N.2
  • 24
    • 0031670372 scopus 로고    scopus 로고
    • β-1,3-Glucanase and resistance to Aspergillus flavus infection in maize
    • Lozovaya, V. V., Waranyuwat, A., and Widholm, J. M. 1998. β-1,3-Glucanase and resistance to Aspergillus flavus infection in maize. Crop Sci. 38:1255-1260.
    • (1998) Crop Sci. , vol.38 , pp. 1255-1260
    • Lozovaya, V.V.1    Waranyuwat, A.2    Widholm, J.M.3
  • 25
    • 84942782727 scopus 로고
    • Antifungal hydrolases in pea tissue. I. Purification and characterization of two chitinases and two β-1,3-glucanases differentially regulated during development and in response to fungal infection
    • Mauch, F., Hadwiger, L. A., and Boller, T. 1988. Antifungal hydrolases in pea tissue. I. Purification and characterization of two chitinases and two β-1,3-glucanases differentially regulated during development and in response to fungal infection. Plant Physiol. 87:325-333.
    • (1988) Plant Physiol. , vol.87 , pp. 325-333
    • Mauch, F.1    Hadwiger, L.A.2    Boller, T.3
  • 26
    • 0001455051 scopus 로고
    • Increased proteinase inhibitor activity in response to infection of resistant tomato plants by Phytophthora infestons
    • Peng, J. H., and Black, L. L. 1976. Increased proteinase inhibitor activity in response to infection of resistant tomato plants by Phytophthora infestons. Phytopathology 66:958-963.
    • (1976) Phytopathology , vol.66 , pp. 958-963
    • Peng, J.H.1    Black, L.L.2
  • 27
    • 0027230258 scopus 로고
    • Overproduction by gene amplification of the multifunctional arom protein confers glyphosate tolerance to a plastid-free mutant of Euglena gracilia
    • Reinbothe, S., Ortel, B., and Parthier, B. 1993. Overproduction by gene amplification of the multifunctional arom protein confers glyphosate tolerance to a plastid-free mutant of Euglena gracilia. Mol. Gen. Genet. 239:416-424.
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 416-424
    • Reinbothe, S.1    Ortel, B.2    Parthier, B.3
  • 28
    • 0001144526 scopus 로고
    • Seed storage proteins: The enzyme inhibitors
    • Richardson, M. 1991. Seed storage proteins: The enzyme inhibitors. Methods Plant Biochem. 5:259-305.
    • (1991) Methods Plant Biochem. , vol.5 , pp. 259-305
    • Richardson, M.1
  • 29
    • 0001068155 scopus 로고
    • A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor
    • Richardson, M., Valdes-Rodriguez, S., and Blanco-Labra, A. 1987. A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor. Nature 327:432-434.
    • (1987) Nature , vol.327 , pp. 432-434
    • Richardson, M.1    Valdes-Rodriguez, S.2    Blanco-Labra, A.3
  • 31
    • 0023052559 scopus 로고
    • Isolation and partial characterization of two antifungal proteins from barley
    • Roberts, W. K., and Selitrennikoff, C. P. 1986. Isolation and partial characterization of two antifungal proteins from barley. Biochirn. Biophys. Acta 880:161-170.
    • (1986) Biochirn. Biophys. Acta , vol.880 , pp. 161-170
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 32
    • 0025063227 scopus 로고
    • Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity
    • Roberts, W. K., and Selitrennikoff, C. P. 1990. Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity. J. Gen. Microbiol. 136:1771-1778.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 1771-1778
    • Roberts, W.K.1    Selitrennikoff, C.P.2
  • 33
    • 0019395972 scopus 로고
    • Natural plant enzyme inhibitors. Characterization of an unusual α-amylase/trypsin inhibitor from ragi (Eleusine coracana Geartn.)
    • Shivaraj, B., and Pattabiraman, T. N. 1981. Natural plant enzyme inhibitors. Characterization of an unusual α-amylase/trypsin inhibitor from ragi (Eleusine coracana Geartn.). Biochem. J. 193:29-36.
    • (1981) Biochem. J. , vol.193 , pp. 29-36
    • Shivaraj, B.1    Pattabiraman, T.N.2
  • 34
    • 0024709804 scopus 로고
    • Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophiluin
    • Smith, L. D., Budgen, N., Bungard, S. J., Danson, M. J., and Hough, D. W. 1989. Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophiluin. Biochem. J. 261:973-977.
    • (1989) Biochem. J. , vol.261 , pp. 973-977
    • Smith, L.D.1    Budgen, N.2    Bungard, S.J.3    Danson, M.J.4    Hough, D.W.5
  • 35
    • 0017691198 scopus 로고
    • Isolation and characterization of trypsin inhibitor from opaque-2 corn seeds
    • Swartz, M. J., Mitchell, H. L., Cox, D. J., and Reeck, G. R. 1977. Isolation and characterization of trypsin inhibitor from opaque-2 corn seeds. J. Biol.Chem. 252:8105-8107.
    • (1977) J. Biol.chem. , vol.252 , pp. 8105-8107
    • Swartz, M.J.1    Mitchell, H.L.2    Cox, D.J.3    Reeck, G.R.4
  • 36
    • 0027132885 scopus 로고
    • Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors
    • Terras, F. R. G., Schoofs, H. M. E., Thevissen, K., Osborn, R. W., Vanderleyden, J., Cammue, B. P. A., and Broekaert, W. F. 1993. Synergistic enhancement of the antifungal activity of wheat and barley thionins by radish and oilseed rape 2S albumins and by barley trypsin inhibitors. Plant Physiol. 103:1311-1319.
    • (1993) Plant Physiol. , vol.103 , pp. 1311-1319
    • Terras, F.R.G.1    Schoofs, H.M.E.2    Thevissen, K.3    Osborn, R.W.4    Vanderleyden, J.5    Cammue, B.P.A.6    Broekaert, W.F.7
  • 37
    • 0031052422 scopus 로고    scopus 로고
    • Inducers of aflatoxin biosynthesis from colonized maize kernels are generated by an amylase activity from Aspergillus flavus
    • Woloshuk, C. P., Cavaletto, J. R., and Cleveland, T. E. 1997. Inducers of aflatoxin biosynthesis from colonized maize kernels are generated by an amylase activity from Aspergillus flavus. Phytopathology 87:164-169.
    • (1997) Phytopathology , vol.87 , pp. 164-169
    • Woloshuk, C.P.1    Cavaletto, J.R.2    Cleveland, T.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.