메뉴 건너뛰기




Volumn 60, Issue 3, 2008, Pages 403-409

Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera: Cerambycidae) larvae

Author keywords

Cerambycid beetle; Midgut peptidases; Morimus funereus; Protease inhibitors; Synthetic substrate; Zymogram

Indexed keywords


EID: 53549104726     PISSN: 03544664     EISSN: None     Source Type: Journal    
DOI: 10.2298/ABS0803403B     Document Type: Article
Times cited : (2)

References (27)
  • 1
    • 53549101870 scopus 로고    scopus 로고
    • Ahmad, S., Brattsen, L. B., Mullin, C. A., and S. U. Yu (1986). enzymes involved in metabolism of plant allochemicals, In: Molecular Aspects of Insect-Plant Oscillations (eds. L. B. Brattsen and S. Ahmad), 73-151. Plenum Press, New York.
    • Ahmad, S., Brattsen, L. B., Mullin, C. A., and S. U. Yu (1986). enzymes involved in metabolism of plant allochemicals, In: Molecular Aspects of Insect-Plant Oscillations (eds. L. B. Brattsen and S. Ahmad), 73-151. Plenum Press, New York.
  • 2
    • 33847646708 scopus 로고    scopus 로고
    • Alcala-Canto, Y., Alberti-Navarro, A., and F. Ibarra-Velarde (2007). Serine protease activity demonstrated in the larval stage of the pentastomid Linguatula serrata. Parasitol. Res. 100, 1011-1014.
    • Alcala-Canto, Y., Alberti-Navarro, A., and F. Ibarra-Velarde (2007). Serine protease activity demonstrated in the larval stage of the pentastomid Linguatula serrata. Parasitol. Res. 100, 1011-1014.
  • 3
    • 53549117414 scopus 로고    scopus 로고
    • Bernays, E. A., and R. F. Chapman (1994). Chemicals in plants, In: Host-Plant Selection by Phytophagous Insects (eds. e. A. Bernays and R. F. Chapman), 14-60. Chapman and Hall, New York.
    • Bernays, E. A., and R. F. Chapman (1994). Chemicals in plants, In: Host-Plant Selection by Phytophagous Insects (eds. e. A. Bernays and R. F. Chapman), 14-60. Chapman and Hall, New York.
  • 4
    • 0030044878 scopus 로고    scopus 로고
    • Blanco-Labra, A., Martinez-Gallardo, N. A., Sandoval-Cardoso, L., and J. Delano-Frier (1996). Purification and characterization of a digestive cathepsin D proteinase isolated from Tribolium castaneum larvae (Herbst). Insect Biochem. Mol. Biol. 26, 95-100.
    • Blanco-Labra, A., Martinez-Gallardo, N. A., Sandoval-Cardoso, L., and J. Delano-Frier (1996). Purification and characterization of a digestive cathepsin D proteinase isolated from Tribolium castaneum larvae (Herbst). Insect Biochem. Mol. Biol. 26, 95-100.
  • 5
    • 39049120322 scopus 로고    scopus 로고
    • Božić, N., Ivanović, J., Nenadović, V., Bergström, J., Larsson, T., and Z. Vujčić (2008). Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. Comp. Biochem. Physiol. 149b, 454-462.
    • Božić, N., Ivanović, J., Nenadović, V., Bergström, J., Larsson, T., and Z. Vujčić (2008). Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. Comp. Biochem. Physiol. 149b, 454-462.
  • 6
    • 0037307262 scopus 로고    scopus 로고
    • Božić, N., Vujčić, Z., Nenadović, V., and J. Ivanović (2003). Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera: Cerambycidae) larvae. Comp. Biochem. Physiol. 134b, 231-241.
    • Božić, N., Vujčić, Z., Nenadović, V., and J. Ivanović (2003). Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera: Cerambycidae) larvae. Comp. Biochem. Physiol. 134b, 231-241.
  • 7
    • 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
  • 8
    • 0036294637 scopus 로고    scopus 로고
    • Bruno, M. A., Pardo, M. F., Caffini, N. O., and L. M. I. Lopez (2002). Purification of a new endopeptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae). Acta Farm. Bonaerense, 21(1), 51-56.
    • Bruno, M. A., Pardo, M. F., Caffini, N. O., and L. M. I. Lopez (2002). Purification of a new endopeptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae). Acta Farm. Bonaerense, 21(1), 51-56.
  • 9
    • 36849076255 scopus 로고    scopus 로고
    • Dojnov, B., Božić, N., Nenadović, V., Ivanović, J., and Z. Vujčić (2008). Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae. Comp. Biochem. Physiol. 149b, 153-160.
    • Dojnov, B., Božić, N., Nenadović, V., Ivanović, J., and Z. Vujčić (2008). Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae. Comp. Biochem. Physiol. 149b, 153-160.
  • 10
    • 53549088009 scopus 로고    scopus 로고
    • Crossed D signurCrossed d signević, A., Vujčić, Z., Jankov, R. M., Nenadović, V., and J. Ivanović (1997). Trypsin-like enzymes from the midgut of Morimus funereus larvae (Coleoptera: Cerambycidae). Arch. Biol. Sci. (Belgrade) 49, 19P-20P.
    • Crossed D signurCrossed d signević, A., Vujčić, Z., Jankov, R. M., Nenadović, V., and J. Ivanović (1997). Trypsin-like enzymes from the midgut of Morimus funereus larvae (Coleoptera: Cerambycidae). Arch. Biol. Sci. (Belgrade) 49, 19P-20P.
  • 11
    • 50549163362 scopus 로고    scopus 로고
    • Erlanger, B. F., Kokowsky, N., and W. Cohen (1961). The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278.
    • Erlanger, B. F., Kokowsky, N., and W. Cohen (1961). The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278.
  • 12
    • 0018854046 scopus 로고
    • electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates
    • Heussen, C., and E. B. Dowdle (1980). electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102, 196-202.
    • (1980) Anal. Biochem , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 13
    • 0016429972 scopus 로고    scopus 로고
    • Ivanović, J. P., Janković-Hladni, M. I., and M. P. Milanović (1975). effect of constant temperature on survival rate, neurosecretion, endocrine cells, and digestive enzymes in Morimus funereus larvae (Cerambycidae: Coleoptera). Comp. Biochem. Physiol. 50a, 125-130.
    • Ivanović, J. P., Janković-Hladni, M. I., and M. P. Milanović (1975). effect of constant temperature on survival rate, neurosecretion, endocrine cells, and digestive enzymes in Morimus funereus larvae (Cerambycidae: Coleoptera). Comp. Biochem. Physiol. 50a, 125-130.
  • 14
    • 0000612288 scopus 로고    scopus 로고
    • Influence of diet and temperature on life cycle of phytophagous insects. A review
    • in Serbian
    • Ivanović, J., and V. Nenadović (1999). Influence of diet and temperature on life cycle of phytophagous insects. A review. (in Serbian). Pesticidi, 14, 309-328.
    • (1999) Pesticidi , vol.14 , pp. 309-328
    • Ivanović, J.1    Nenadović, V.2
  • 15
    • 0035989452 scopus 로고    scopus 로고
    • Ivanović, J., Crossed D signorCrossed d signević, S., Ilijin, L., Janković-Tomanić, M., and V, nenadović (2002). Metabolic response of cerambycid beetle (Morimus funereus) larvae to starvation and food quality. Comp. Biochem. Physiol. 132a, 555-566.
    • Ivanović, J., Crossed D signorCrossed d signević, S., Ilijin, L., Janković-Tomanić, M., and V, nenadović (2002). Metabolic response of cerambycid beetle (Morimus funereus) larvae to starvation and food quality. Comp. Biochem. Physiol. 132a, 555-566.
  • 16
    • 53549088282 scopus 로고    scopus 로고
    • Ivanović, J., Janković-Hladni, M., Nenadović, V., Frušić, M., and V. Stanić (1988). endocrinological and biochemical aspects of stress and adaptations of phytophagaous insects to environmental changes, In: Endocrinological Frontiers in Physiological Insects Ecology (eds. F. Z. Sehnal, A. Zabža, and D. Denlinger), 141-159. Wroclaw Technical Press, Wroclaw.
    • Ivanović, J., Janković-Hladni, M., Nenadović, V., Frušić, M., and V. Stanić (1988). endocrinological and biochemical aspects of stress and adaptations of phytophagaous insects to environmental changes, In: Endocrinological Frontiers in Physiological Insects Ecology (eds. F. Z. Sehnal, A. Zabža, and D. Denlinger), 141-159. Wroclaw Technical Press, Wroclaw.
  • 17
    • 0031260101 scopus 로고    scopus 로고
    • The adaptation of insects to plant protease inhibitors
    • Jongsma, M. A., and C. Bolter (1997). The adaptation of insects to plant protease inhibitors. J. Insect Physiol. 43, 885-895.
    • (1997) J. Insect Physiol , vol.43 , pp. 885-895
    • Jongsma, M.A.1    Bolter, C.2
  • 18
    • 0000934903 scopus 로고    scopus 로고
    • Kwan, K. K. H., Nakai, S., and J. Skura (1983). Comparison of four methods for determining protease activity in milk. J. Food Sci. 48, 1418-1421.
    • Kwan, K. K. H., Nakai, S., and J. Skura (1983). Comparison of four methods for determining protease activity in milk. J. Food Sci. 48, 1418-1421.
  • 19
    • 0029109349 scopus 로고
    • Characterization of midgut exopeptidase activity from larval Spodoptera littoralis
    • Lee, M. J., and J. H. Anstee (1995). Characterization of midgut exopeptidase activity from larval Spodoptera littoralis. Insect Biochem. Mol. Biol. 25, 63-71.
    • (1995) Insect Biochem. Mol. Biol , vol.25 , pp. 63-71
    • Lee, M.J.1    Anstee, J.H.2
  • 20
    • 0000698945 scopus 로고
    • Herbivory in relation to plant nitrogen content
    • Mattson, W. J. (1980). Herbivory in relation to plant nitrogen content. Ann. Rev. Ecol. Syst. 11, 119-161.
    • (1980) Ann. Rev. Ecol. Syst , vol.11 , pp. 119-161
    • Mattson, W.J.1
  • 21
    • 53549097022 scopus 로고    scopus 로고
    • Nenadović, V., Janković-Hladni, M., Prolić, Z., and J. Ivanović (1994). Metabolic response of Morimus funereus and Cerambux cerdo larvae to low temperature, In: Plant Protection Today and Tomorrow (eds. M. Šestović, N. K. Nešković, and I. Perić), 303-314. Društvo za zaštitu bilja Srbije, Beograd, (In Serbian).
    • Nenadović, V., Janković-Hladni, M., Prolić, Z., and J. Ivanović (1994). Metabolic response of Morimus funereus and Cerambux cerdo larvae to low temperature, In: Plant Protection Today and Tomorrow (eds. M. Šestović, N. K. Nešković, and I. Perić), 303-314. Društvo za zaštitu bilja Srbije, Beograd, (In Serbian).
  • 22
    • 0000316764 scopus 로고    scopus 로고
    • Novillo, C., Castanera, P., and F. Ortego (1997). Characterization and distribution of chymotrypsin-like and other digestive proteases in Colorado potato beetle larvae. Arch. Insect Biochem. Physiol. 36, 181-201.
    • Novillo, C., Castanera, P., and F. Ortego (1997). Characterization and distribution of chymotrypsin-like and other digestive proteases in Colorado potato beetle larvae. Arch. Insect Biochem. Physiol. 36, 181-201.
  • 23
    • 53549126591 scopus 로고    scopus 로고
    • Reeck, G., Oppert, B., Denton, M., Kanost, M., Baker, J. E., and K. J. Kramer (1999). Insect proteinases, In: Proteases: New Perspectives (Ed. V. Turk), 125-148. Birkhauser Verlag, Basel, Boston, Berlin.
    • Reeck, G., Oppert, B., Denton, M., Kanost, M., Baker, J. E., and K. J. Kramer (1999). Insect proteinases, In: Proteases: New Perspectives (Ed. V. Turk), 125-148. Birkhauser Verlag, Basel, Boston, Berlin.
  • 24
    • 0002008198 scopus 로고
    • Proteinase inhibitors
    • eds. G. A. Rosenthal and D. H. Jensen, Academic Press, New York
    • Ryan, C. N. (1980). Proteinase inhibitors, In: Herbivores: Their nteraction with Secondary Plant Metabolites (eds. G. A. Rosenthal and D. H. Jensen), 599-618. Academic Press, New York.
    • (1980) Herbivores: Their nteraction with Secondary Plant Metabolites , pp. 599-618
    • Ryan, C.N.1
  • 25
    • 19344372284 scopus 로고    scopus 로고
    • Telang, M. A., Giri, A. P., Sainani, M. N., and V. S. Gupta (2005). Characterization of two midgut proteinases of Helicoverpa armigera and their interaction with proteinase inhibitors. J. Insect Physiol. 51, 513-522.
    • Telang, M. A., Giri, A. P., Sainani, M. N., and V. S. Gupta (2005). Characterization of two midgut proteinases of Helicoverpa armigera and their interaction with proteinase inhibitors. J. Insect Physiol. 51, 513-522.
  • 26
    • 0027999854 scopus 로고
    • Insect digestive enzymes: Properties, compartmentalization and function
    • Terra, W. R., and C. Ferreira (1994). Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 109b, 1-62.
    • (1994) Comp. Biochem. Physiol , vol.109 b , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 27
    • 0001418289 scopus 로고
    • Isolation and partial characterization of a major gut proteinase from larval Acanthoscelides obtectus Say (Coleoptera, Bruchidae)
    • Wieman, K. F., and S. S. Nielsen (1988). Isolation and partial characterization of a major gut proteinase from larval Acanthoscelides obtectus Say (Coleoptera, Bruchidae). Comp. Biochem. Physiol. 89B, 419-426.
    • (1988) Comp. Biochem. Physiol , vol.89 B , pp. 419-426
    • Wieman, K.F.1    Nielsen, S.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.