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Volumn 149, Issue 1, 2008, Pages 153-160

Purification and properties of midgut α-amylase isolated from Morimus funereus (Coleoptera: Cerambycidae) larvae

Author keywords

Cerambycid beetle; Isoform; Midgut amylase; Morimus funereus; Xylophagous larvae

Indexed keywords

AMYLASE; CALCIUM CHLORIDE; ISOENZYME; POTATO STARCH; SODIUM CHLORIDE;

EID: 36849076255     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2007.09.009     Document Type: Article
Times cited : (42)

References (35)
  • 1
    • 0009505792 scopus 로고
    • Studies on the midgut amylase activity of Tenebrio molitor L. larvae
    • Applebaum S.W., Janković M., and Birk Y. Studies on the midgut amylase activity of Tenebrio molitor L. larvae. J. Insect Physiol. 7 (1961) 100-108
    • (1961) J. Insect Physiol. , vol.7 , pp. 100-108
    • Applebaum, S.W.1    Janković, M.2    Birk, Y.3
  • 2
    • 0344662855 scopus 로고
    • Purification and partial characterization of a-amylase allozymes from the lesser grain borer, Rhyzopertha dominica
    • Baker J.E. Purification and partial characterization of a-amylase allozymes from the lesser grain borer, Rhyzopertha dominica. Insect Biochem. 21 (1991) 303-311
    • (1991) Insect Biochem. , vol.21 , pp. 303-311
    • Baker, J.E.1
  • 3
    • 33748037939 scopus 로고
    • Amylases, α and β
    • De Murray P. (Ed), Deutcher Acad. Press INC, San Diego California
    • Bernfeld P. Amylases, α and β. In: De Murray P. (Ed). Methods in enzymology vol. I (1955), Deutcher Acad. Press INC, San Diego California 149-158
    • (1955) Methods in enzymology , vol.I , pp. 149-158
    • Bernfeld, P.1
  • 4
    • 0037307262 scopus 로고    scopus 로고
    • Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera: Cerambycidae) larvae
    • Božić N., Vujčić Z., Nenadović V., and Ivanović J. Partial purification and characterization of midgut leucyl aminopeptidase of Morimus funereus (Coleoptera: Cerambycidae) larvae. Comp. Biochem. Physiol. 134B (2003) 231-234
    • (2003) Comp. Biochem. Physiol. , vol.134 B , pp. 231-234
    • Božić, N.1    Vujčić, Z.2    Nenadović, V.3    Ivanović, J.4
  • 5
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0017285772 scopus 로고
    • Physical and catalytic properties of α-amylase from Tenebrio molitor L. larvae
    • Buonocore V., Poeiro E., Silano V., and Tomasi M. Physical and catalytic properties of α-amylase from Tenebrio molitor L. larvae. Biochem. J. 153 (1976) 621-625
    • (1976) Biochem. J. , vol.153 , pp. 621-625
    • Buonocore, V.1    Poeiro, E.2    Silano, V.3    Tomasi, M.4
  • 7
    • 0000549241 scopus 로고
    • Resolution and partial characterization of proteinases and α-amylases from midguts of larvae of the bruchid beetle Callosobruchus maculatus (F.)
    • Campos F.A.P., Xavier-Filho J., Silva C.P., and Ary M.B. Resolution and partial characterization of proteinases and α-amylases from midguts of larvae of the bruchid beetle Callosobruchus maculatus (F.). Comp. Biochem. Physiol. 92B (1989) 51-57
    • (1989) Comp. Biochem. Physiol. , vol.92 B , pp. 51-57
    • Campos, F.A.P.1    Xavier-Filho, J.2    Silva, C.P.3    Ary, M.B.4
  • 8
    • 34248664687 scopus 로고    scopus 로고
    • α-Amylase activity of Rhyzopertha dominica (Coleoptera: Bostrichidae) reared on several wheat varieties and its inhibition with kernel extracts
    • Cinco-Moroyoqui F.J., Rosas-Burgos E.C., Borboa-Flores J., and Cortez-Rocha M.O. α-Amylase activity of Rhyzopertha dominica (Coleoptera: Bostrichidae) reared on several wheat varieties and its inhibition with kernel extracts. J. Econ. Entomol. 99 6 (2006) 2146-2150
    • (2006) J. Econ. Entomol. , vol.99 , Issue.6 , pp. 2146-2150
    • Cinco-Moroyoqui, F.J.1    Rosas-Burgos, E.C.2    Borboa-Flores, J.3    Cortez-Rocha, M.O.4
  • 9
    • 0242308225 scopus 로고
    • Survey and electrophoretical separation of the glycosidases of Rhagium inquisitor (Coleoptera: Cerambycidae) larvae
    • Chipoulet J.M., and Chararas C. Survey and electrophoretical separation of the glycosidases of Rhagium inquisitor (Coleoptera: Cerambycidae) larvae. Comp. Biochem. Physiol. 80B (1985) 241-246
    • (1985) Comp. Biochem. Physiol. , vol.80 B , pp. 241-246
    • Chipoulet, J.M.1    Chararas, C.2
  • 11
    • 78651153791 scopus 로고
    • Disc electrophoresis-II: method and application to human serum proteins
    • Davis B.J. Disc electrophoresis-II: method and application to human serum proteins. Ann. N.Y. Acad. Sci. 121 (1964) 404-427
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 13
    • 36849058842 scopus 로고    scopus 로고
    • Extraction, purification, and inhibitory effect of alpha-amylase inhibitor from wheat (Triticum aestivum Var. Zarrin)
    • Heidari R., Zareae S., and Heidarizadeh M. Extraction, purification, and inhibitory effect of alpha-amylase inhibitor from wheat (Triticum aestivum Var. Zarrin). Pakistan J. Nutr. 4 2 (2005) 101-105
    • (2005) Pakistan J. Nutr. , vol.4 , Issue.2 , pp. 101-105
    • Heidari, R.1    Zareae, S.2    Heidarizadeh, M.3
  • 14
    • 36849008790 scopus 로고
    • Distribution and some characteristics of intestinal amylases in xylophagous larvae of ecologically equivalent species
    • Ivanović J., and Milanović M. Distribution and some characteristics of intestinal amylases in xylophagous larvae of ecologically equivalent species. Ekologija 2 1-2 (1967) 177-188
    • (1967) Ekologija , vol.2 , Issue.1-2 , pp. 177-188
    • Ivanović, J.1    Milanović, M.2
  • 15
    • 36849004599 scopus 로고
    • Basis of the olygophagy of the species Morimus funereus
    • Ivanović J. Basis of the olygophagy of the species Morimus funereus. Archiv. Biol. Sci. 20 (1970) 53-57
    • (1970) Archiv. Biol. Sci. , vol.20 , pp. 53-57
    • Ivanović, J.1
  • 16
    • 0346395365 scopus 로고
    • Individual variability of the pH optimum of amylase in larval populations of the insect species Morimus funereus L
    • Ivanović J., and Marinković D. Individual variability of the pH optimum of amylase in larval populations of the insect species Morimus funereus L. Genetika 2 (1970) 105-111
    • (1970) Genetika , vol.2 , pp. 105-111
    • Ivanović, J.1    Marinković, D.2
  • 17
    • 85051611676 scopus 로고
    • Metabolic response to stressors
    • Ivanović J., and Janković-Hladni M. (Eds), CRC Press
    • Ivanović J. Metabolic response to stressors. In: Ivanović J., and Janković-Hladni M. (Eds). Hormones and Metabolism in Insect Stress (1991), CRC Press 27-69
    • (1991) Hormones and Metabolism in Insect Stress , pp. 27-69
    • Ivanović, J.1
  • 18
    • 36849069583 scopus 로고
    • Some characteristics of the larval midgut amylase of members of the family Cerambycidae during the first decomposition phase of a deciduous trunk
    • Janković M., Ivanović J., and Marinković D. Some characteristics of the larval midgut amylase of members of the family Cerambycidae during the first decomposition phase of a deciduous trunk. Archiv. Biol. Sci. 18 (1967) 39-45
    • (1967) Archiv. Biol. Sci. , vol.18 , pp. 39-45
    • Janković, M.1    Ivanović, J.2    Marinković, D.3
  • 19
    • 0001130394 scopus 로고
    • Proteinases and amylases of larval midgut of Zabrotes subfasciatus reared on cowpea (Vigna unguiculata) seeds
    • Lemos F.J.A., Campos F.A.P., Silva C.P., and Xavier-Filho J. Proteinases and amylases of larval midgut of Zabrotes subfasciatus reared on cowpea (Vigna unguiculata) seeds. Entmol. Exp. Appl. 56 (1990) 219-227
    • (1990) Entmol. Exp. Appl. , vol.56 , pp. 219-227
    • Lemos, F.J.A.1    Campos, F.A.P.2    Silva, C.P.3    Xavier-Filho, J.4
  • 20
    • 23444453211 scopus 로고    scopus 로고
    • Two forms of α-amylase in mantle tissue of Mytilus galloprovincialis: purification and molecular properties of form II
    • Lombraña M., Suárez P., and San Juan F. Two forms of α-amylase in mantle tissue of Mytilus galloprovincialis: purification and molecular properties of form II. Comp. Biochem. Physiol. 142B (2005) 56-66
    • (2005) Comp. Biochem. Physiol. , vol.142 B , pp. 56-66
    • Lombraña, M.1    Suárez, P.2    San Juan, F.3
  • 21
    • 0024514666 scopus 로고
    • A super-secondary structure predicted to be common to several α-1,4-d-glucan-cleaving enzymes
    • MacGregor E.A., and Svensson B. A super-secondary structure predicted to be common to several α-1,4-d-glucan-cleaving enzymes. Biochem. J. 259 (1989) 145-152
    • (1989) Biochem. J. , vol.259 , pp. 145-152
    • MacGregor, E.A.1    Svensson, B.2
  • 24
    • 0014973926 scopus 로고
    • The α-amylase of the beetle Callosobruchus chinensis
    • Podoler H., and Applebaum S.W. The α-amylase of the beetle Callosobruchus chinensis. Biochem. J. 121 (1971) 321-325
    • (1971) Biochem. J. , vol.121 , pp. 321-325
    • Podoler, H.1    Applebaum, S.W.2
  • 25
    • 0032922796 scopus 로고    scopus 로고
    • Digestion in larvae of Callosobruchus maculatus and Zabrotes subfasciatus (Coleoptera: Bruchidae) with emphasis on α-amylases and oligosaccharidases
    • Silva C.P., Terra W.R., Xavier-Filho J., Grossi de Sá M.F., Lopes A.R., and Pontes E.G. Digestion in larvae of Callosobruchus maculatus and Zabrotes subfasciatus (Coleoptera: Bruchidae) with emphasis on α-amylases and oligosaccharidases. Insect Biochem. Mol. Biol. 29 (1999) 355-366
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 355-366
    • Silva, C.P.1    Terra, W.R.2    Xavier-Filho, J.3    Grossi de Sá, M.F.4    Lopes, A.R.5    Pontes, E.G.6
  • 27
    • 0034766274 scopus 로고    scopus 로고
    • Induction of digestive α-amylase in larvae of Zabrotes subfasciatus (Coleoptera: Bruchidae) in response to ingestion of common bean α-amylase inhibitor 1
    • Silva C.P., Terra W.R., de Sá M.F.G., Samuels R.I., Isejima E.M., Bifano T.D., and Almeida J.S. Induction of digestive α-amylase in larvae of Zabrotes subfasciatus (Coleoptera: Bruchidae) in response to ingestion of common bean α-amylase inhibitor 1. J. Insect Physiol. 47 (2001) 1283-1290
    • (2001) J. Insect Physiol. , vol.47 , pp. 1283-1290
    • Silva, C.P.1    Terra, W.R.2    de Sá, M.F.G.3    Samuels, R.I.4    Isejima, E.M.5    Bifano, T.D.6    Almeida, J.S.7
  • 28
    • 0027999854 scopus 로고
    • Insect digestive enzymes: properties, compartmentalization and function
    • Terra W.R., and Ferreira C. Insect digestive enzymes: properties, compartmentalization and function. Comp. Biochem. Physiol. 109B (1994) 1-62
    • (1994) Comp. Biochem. Physiol. , vol.109 B , pp. 1-62
    • Terra, W.R.1    Ferreira, C.2
  • 29
  • 30
    • 0034059676 scopus 로고    scopus 로고
    • α-Amylases of the coffee berry borer (Hypothenemus hampei) and their inhibition by two plant amylase inhibitors
    • Valencia A., Bustillo A.E., Ossa G.E., and Chrispeels M. α-Amylases of the coffee berry borer (Hypothenemus hampei) and their inhibition by two plant amylase inhibitors. Insect Biochem. Mol. Biol. 30 (2000) 207-213
    • (2000) Insect Biochem. Mol. Biol. , vol.30 , pp. 207-213
    • Valencia, A.1    Bustillo, A.E.2    Ossa, G.E.3    Chrispeels, M.4
  • 32
    • 0036015624 scopus 로고    scopus 로고
    • Characterization of the proteolytic enzymes in the midgut of the European cockchafer, Melolontha melolontha (Coleoptera: Scarabaeidae)
    • Wagner W., Möhrlen F., and Schnetter W. Characterization of the proteolytic enzymes in the midgut of the European cockchafer, Melolontha melolontha (Coleoptera: Scarabaeidae). Insect Biochem. Mol. Biol. 32 (2002) 803-814
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 803-814
    • Wagner, W.1    Möhrlen, F.2    Schnetter, W.3
  • 34
    • 0001272522 scopus 로고
    • Partial purification and characterization of the major endoamylase of mature pea leaves
    • Ziegler P. Partial purification and characterization of the major endoamylase of mature pea leaves. Plant Physiol. 86 (1988) 659-666
    • (1988) Plant Physiol. , vol.86 , pp. 659-666
    • Ziegler, P.1
  • 35
    • 0037223984 scopus 로고    scopus 로고
    • Enzymes for digestion of cellulose and other polysaccharide in the gut of longhorn beetle larvae, Rhagium inquisitor L. (Col., Cerambycidae)
    • Zverlov V.V., Höll W., and Schwarz W.H. Enzymes for digestion of cellulose and other polysaccharide in the gut of longhorn beetle larvae, Rhagium inquisitor L. (Col., Cerambycidae). Internat. Biodeter. Biodeg. 51 (2003) 175-179
    • (2003) Internat. Biodeter. Biodeg. , vol.51 , pp. 175-179
    • Zverlov, V.V.1    Höll, W.2    Schwarz, W.H.3


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