메뉴 건너뛰기




Volumn 38, Issue 11, 2005, Pages 1633-1641

Perspectives of digestive pest control with proteinase inhibitors that mainly affect the trypsin-like activity of Anticarsia gemmatalis Hübner (Lepidoptera: Noctuidae)

Author keywords

Anticarsia gemmatalis (Lepidoptera: Noctuidae); Azocasein hydrolysis; BApNA hydrolysis; Protein digestion; Proteinase inhibitors; Serine proteinases

Indexed keywords

BENZAMIDINE; BENZYLSULFONYL FLUORIDE; CYSTEINE PROTEINASE; MERCAPTOETHANOL; PROTEINASE INHIBITOR; SERINE PROTEINASE; SODIUM CHLORIDE; TRYPSIN;

EID: 27944443237     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/S0100-879X2005001100010     Document Type: Article
Times cited : (14)

References (40)
  • 3
    • 0001526906 scopus 로고    scopus 로고
    • Classical biological control in an ephemeral crop habitat with Anticarsia gemmatalis nucleopolyhedrovirus
    • Fuxa JR & Richter AR (1999). Classical biological control in an ephemeral crop habitat with Anticarsia gemmatalis nucleopolyhedrovirus. Biocontrol, 44: 405-421.
    • (1999) Biocontrol , vol.44 , pp. 405-421
    • Fuxa, J.R.1    Richter, A.R.2
  • 5
    • 0031843004 scopus 로고    scopus 로고
    • Construction of occluded recombinant baculoviruses containing the full-length cry1Ab and cry1Ac genes from Bacillus thuringiensis
    • Ribeiro BM & Crook NE (1998). Construction of occluded recombinant baculoviruses containing the full-length cry1Ab and cry1Ac genes from Bacillus thuringiensis. Brazilian Journal of Medical and Biological Research, 31: 763-769.
    • (1998) Brazilian Journal of Medical and Biological Research , vol.31 , pp. 763-769
    • Ribeiro, B.M.1    Crook, N.E.2
  • 6
    • 0031887585 scopus 로고    scopus 로고
    • Identifying proteins with insecticidal activity: Use of encoding genes to produce insect-resistant transgenic crops
    • Gatehouse AMR & Gatehouse JA (1998). Identifying proteins with insecticidal activity: use of encoding genes to produce insect-resistant transgenic crops. Pesticide Science, 52: 165-175.
    • (1998) Pesticide Science , vol.52 , pp. 165-175
    • Gatehouse, A.M.R.1    Gatehouse, J.A.2
  • 7
    • 0000180578 scopus 로고
    • Proteinase inhibitors in plants: Genes improving defenses against insects and pathogens
    • Ryan CA (1990). Proteinase inhibitors in plants: genes improving defenses against insects and pathogens. Annual Review of Phytopathology, 28: 425-449.
    • (1990) Annual Review of Phytopathology , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 9
    • 0023652138 scopus 로고
    • A novel mechanism for insect resistance engineered into tobacco
    • Hilder VA, Gatehouse AMR, Sheerman SE et al. (1987). A novel mechanism for insect resistance engineered into tobacco. Nature, 330: 160-163.
    • (1987) Nature , vol.330 , pp. 160-163
    • Hilder, V.A.1    Gatehouse, A.M.R.2    Sheerman, S.E.3
  • 10
    • 0027833635 scopus 로고
    • Effects of soybean protease inhibitors on the growth and development of larval Helicoverpa armigera
    • Johnston KA, Gatehouse JA & Anstee JH (1993). Effects of soybean protease inhibitors on the growth and development of larval Helicoverpa armigera. Journal of Insect Physiology, 39: 657-664.
    • (1993) Journal of Insect Physiology , vol.39 , pp. 657-664
    • Johnston, K.A.1    Gatehouse, J.A.2    Anstee, J.H.3
  • 11
    • 0031239547 scopus 로고    scopus 로고
    • Proteinase inhibitors from Nicotiana alata enhance plant resistance to insect pests
    • Heath RL, McDonald G, Christeller JT et al. (1997). Proteinase inhibitors from Nicotiana alata enhance plant resistance to insect pests. Journal of Insect Physiology, 43: 833-842.
    • (1997) Journal of Insect Physiology , vol.43 , pp. 833-842
    • Heath, R.L.1    McDonald, G.2    Christeller, J.T.3
  • 12
    • 0002818604 scopus 로고    scopus 로고
    • Transgenic potato plants with enhanced resistance to the tomato moth, Lacanobia oleracea: Growth room trials
    • Gatehouse AMR, Davison GM, Newell CA et al. (1997). Transgenic potato plants with enhanced resistance to the tomato moth, Lacanobia oleracea: growth room trials. Molecular Breeding, 3: 49-63.
    • (1997) Molecular Breeding , vol.3 , pp. 49-63
    • Gatehouse, A.M.R.1    Davison, G.M.2    Newell, C.A.3
  • 13
    • 0033016160 scopus 로고    scopus 로고
    • Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleracea; effects of plant protease inhibitors in vitro and in vivo
    • Gatehouse AMR, Norton E, Davison GM et al. (1999). Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleracea; effects of plant protease inhibitors in vitro and in vivo. Journal of Insect Physiology, 45: 545-558.
    • (1999) Journal of Insect Physiology , vol.45 , pp. 545-558
    • Gatehouse, A.M.R.1    Norton, E.2    Davison, G.M.3
  • 14
    • 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 RM & Duffey SS (1986). Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exiqua. Journal of Insect Physiology, 32: 827-833.
    • (1986) Journal of Insect Physiology , vol.32 , pp. 827-833
    • Broadway, R.M.1    Duffey, S.S.2
  • 15
    • 0027999854 scopus 로고
    • Insect digestive enzymes: Properties, compartmentalization and function
    • Terra WR & Ferreira C (1994). Insect digestive enzymes: properties, compartmentalization and function. Comparative Biochemistry and Physiology, 109B: 1-62.
    • (1994) Comparative Biochemistry and Physiology , vol.109 B , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 17
    • 0027661652 scopus 로고
    • Purification and characterization of a trypsin-like digestive enzyme from spruce budworm (Choristoneura fumiferana) responsible for the activation of δ-endotoxin from Bacillus thuringiensis
    • Milne R & Kaplan H (1993). Purification and characterization of a trypsin-like digestive enzyme from spruce budworm (Choristoneura fumiferana) responsible for the activation of δ-endotoxin from Bacillus thuringiensis. Insect Biochemistry and Molecular Biology, 6: 665-673.
    • (1993) Insect Biochemistry and Molecular Biology , vol.6 , pp. 665-673
    • Milne, R.1    Kaplan, H.2
  • 18
    • 0036381690 scopus 로고    scopus 로고
    • Characterization of two Bacillus thuringiensis isolates from South Brazil and their toxicity against Anticarcia gemmatalis (Lepidoptera: Noctuidae)
    • Bobrowski VL, Pasquali G, Bodanese-Zanettini MH et al. (2002). Characterization of two Bacillus thuringiensis isolates from South Brazil and their toxicity against Anticarcia gemmatalis (Lepidoptera: Noctuidae). Biological Control, 25: 129-135.
    • (2002) Biological Control , vol.25 , pp. 129-135
    • Bobrowski, V.L.1    Pasquali, G.2    Bodanese-Zanettini, M.H.3
  • 20
    • 0032029879 scopus 로고    scopus 로고
    • Characterisation of the midgut digestive proteinase activity of the two-spot ladybird (Adalia bipunctata L.) and its sensitivity to proteinase inhibitors
    • Walker AJ, Ford L, Majerus MEN et al. (1998). Characterisation of the midgut digestive proteinase activity of the two-spot ladybird (Adalia bipunctata L.) and its sensitivity to proteinase inhibitors. Insect Biochemistry and Molecular Biology, 28: 173-180.
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , pp. 173-180
    • Walker, A.J.1    Ford, L.2    Majerus, M.E.N.3
  • 21
    • 0031876502 scopus 로고    scopus 로고
    • Isolation and partial characterization of two trypsins from the larval midgut of Spodoptera littoralis (Boisduval)
    • Marchetti S, Chiabà C, Chiesa F et al. (1998). Isolation and partial characterization of two trypsins from the larval midgut of Spodoptera littoralis (Boisduval). Insect Biochemistry and Molecular Biology, 28: 449-458.
    • (1998) Insect Biochemistry and Molecular Biology , vol.28 , pp. 449-458
    • Marchetti, S.1    Chiabà, C.2    Chiesa, F.3
  • 23
    • 0001701325 scopus 로고
    • Midgut protease activities in 12 phytophagous lepidopteran larvae: Dietary and protease inhibitor interactions
    • Christeller JT, Laing WA, Markwick NP et al. (1992). Midgut protease activities in 12 phytophagous lepidopteran larvae: dietary and protease inhibitor interactions. Insect Biochemistry and Molecular Biology, 22: 735-746.
    • (1992) Insect Biochemistry and Molecular Biology , vol.22 , pp. 735-746
    • Christeller, J.T.1    Laing, W.A.2    Markwick, N.P.3
  • 24
    • 0011447254 scopus 로고
    • Proteolytic activity in the digestive fluid in larvae of Trichoplusia ni
    • Pritchett DW, Young SY & Geren CR (1981). Proteolytic activity in the digestive fluid in larvae of Trichoplusia ni. Insect Biochemistry, 11: 523-526.
    • (1981) Insect Biochemistry , vol.11 , pp. 523-526
    • Pritchett, D.W.1    Young, S.Y.2    Geren, C.R.3
  • 26
    • 0000017524 scopus 로고
    • Partial purification and characterization of the major midgut proteases of grass grub larvae (Costelytra zealandica, Coleoptera: Scarabaeidae)
    • Christeller JT, Shaw BD, Gardiner SE et al. (1989). Partial purification and characterization of the major midgut proteases of grass grub larvae (Costelytra zealandica, Coleoptera: Scarabaeidae). Insect Biochemistry, 19: 221-231.
    • (1989) Insect Biochemistry , vol.19 , pp. 221-231
    • Christeller, J.T.1    Shaw, B.D.2    Gardiner, S.E.3
  • 27
    • 0029152568 scopus 로고
    • Endoproteases from the midgut of larval Spodoptera littoralis include a chymotrypsin-like enzyme with an extended binding site
    • Lee MJ & Anstee JH (1995). Endoproteases from the midgut of larval Spodoptera littoralis include a chymotrypsin-like enzyme with an extended binding site. Insect Biochemistry and Molecular Biology, 25: 49-61.
    • (1995) Insect Biochemistry and Molecular Biology , vol.25 , pp. 49-61
    • Lee, M.J.1    Anstee, J.H.2
  • 28
    • 0031177988 scopus 로고    scopus 로고
    • Differentially regulated inhibitor-sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families
    • Brown DP, Wilkinson HS & Gatehouse JA (1997). Differentially regulated inhibitor-sensitive and insensitive protease genes from the phytophagous insect pest, Helicoverpa armigera, are members of complex multigene families. Insect Biochemistry and Molecular Biology, 27: 625-638.
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , pp. 625-638
    • Brown, D.P.1    Wilkinson, H.S.2    Gatehouse, J.A.3
  • 29
    • 0004262303 scopus 로고
    • 2nd edn. Longmans, Green and Co., Ltd., London, UK
    • Dixon M & Webb EC (1964). Enzymes. 2nd edn. Longmans, Green and Co., Ltd., London, UK.
    • (1964) Enzymes
    • Dixon, M.1    Webb, E.C.2
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72: 255-260.
    • (1976) Analytical Biochemistry , vol.72 , pp. 255-260
    • Bradford, M.M.1
  • 31
    • 0024199846 scopus 로고
    • Physiology and biochemistry of insect digestion: An evolutionary perspective
    • Terra WR (1988). Physiology and biochemistry of insect digestion: an evolutionary perspective. Brazilian Journal of Medical and Biological Research, 21: 675-734.
    • (1988) Brazilian Journal of Medical and Biological Research , vol.21 , pp. 675-734
    • Terra, W.R.1
  • 32
    • 0029138570 scopus 로고
    • Protease activities in the larval midgut of Heliothis virescens: Evidence for trypsin and chymotrypsin-like enzymes
    • Johnston KA, Lee MJ, Brough C et al. (1995). Protease activities in the larval midgut of Heliothis virescens: evidence for trypsin and chymotrypsin-like enzymes. Insect Biochemistry and Molecular Biology, 25: 375-383.
    • (1995) Insect Biochemistry and Molecular Biology , vol.25 , pp. 375-383
    • Johnston, K.A.1    Lee, M.J.2    Brough, C.3
  • 36
    • 0001669768 scopus 로고
    • The partial purification and characterization of serine protease activity in midgut of larval Heticoverpa armigera
    • Johnston KA, Lee MJ, Gatehouse JA et al. (1991). The partial purification and characterization of serine protease activity in midgut of larval Heticoverpa armigera. Insect Biochemistry, 21: 389-397.
    • (1991) Insect Biochemistry , vol.21 , pp. 389-397
    • Johnston, K.A.1    Lee, M.J.2    Gatehouse, J.A.3
  • 37
    • 0030239950 scopus 로고    scopus 로고
    • Isolation and some molecular properties of a trypsin-like enzyme from larvae of European corn borer Ostrinia nubilalis Hübner (Lepidoptera: Pyralidae)
    • Bernardi B, Tedeschi G, Ronchi S et al. (1996). Isolation and some molecular properties of a trypsin-like enzyme from larvae of European corn borer Ostrinia nubilalis Hübner (Lepidoptera: Pyralidae). Insect Biochemistry and Molecular Biology, 26: 883-889.
    • (1996) Insect Biochemistry and Molecular Biology , vol.26 , pp. 883-889
    • Bernardi, B.1    Tedeschi, G.2    Ronchi, S.3
  • 40
    • 0000610970 scopus 로고
    • Partial characterization of proteinase activity in the larval midgut of the European corn borer, Ostrinia nubilalis Hübner (Lepidoptera: Pyralidae)
    • Houseman JG, Philogène BJR & Downe AER (1989). Partial characterization of proteinase activity in the larval midgut of the European corn borer, Ostrinia nubilalis Hübner (Lepidoptera: Pyralidae). Canadian Journal of Zoology, 67: 864-867.
    • (1989) Canadian Journal of Zoology , vol.67 , pp. 864-867
    • Houseman, J.G.1    Philogène, B.J.R.2    Downe, A.E.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.