메뉴 건너뛰기




Volumn 70, Issue 1, 2006, Pages 252-262

Purification and characterization of a novel isozyme of chitinase from Bombyx mori

Author keywords

Bombyx mori; Chitinase; Kinetics; Properties; Purification

Indexed keywords

AMINO ACIDS; BIOCONTROL; CHROMATOGRAPHIC ANALYSIS; HYDROLYSIS; HYDROXYAPATITE; PH EFFECTS; PURIFICATION;

EID: 31444440508     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70.252     Document Type: Article
Times cited : (21)

References (60)
  • 1
    • 0000368935 scopus 로고
    • Fungal cell walls: A survey
    • eds. Tanner, W., and Loewus, F. A., Springer-Verlag, Berlin
    • Wessels, J. G. H., and Sietsma, J. H., Fungal cell walls: a survey. In "Plant Carbohydrates II", eds. Tanner, W., and Loewus, F. A., Springer-Verlag, Berlin, pp. 352-394 (1981).
    • (1981) Plant Carbohydrates II , pp. 352-394
    • Wessels, J.G.H.1    Sietsma, J.H.2
  • 2
    • 0000749772 scopus 로고
    • Insect chitin: Physical state, synthesis, degradation and metabolic regulation
    • Kramer, K. J., and Koga, D., Insect chitin: physical state, synthesis, degradation and metabolic regulation. Insect Biochem., 16, 851-877 (1986).
    • (1986) Insect Biochem. , vol.16 , pp. 851-877
    • Kramer, K.J.1    Koga, D.2
  • 3
    • 0037085189 scopus 로고    scopus 로고
    • Chitin production by arthropods in the hydrosphere
    • Cauchie, H.-M., Chitin production by arthropods in the hydrosphere. Hydrobiologia, 470, 63-96 (2002).
    • (2002) Hydrobiologia , vol.470 , pp. 63-96
    • Cauchie, H.-M.1
  • 4
    • 0346399742 scopus 로고    scopus 로고
    • Chitin metabolism in insects: Structure, function and regulation of chitin synthases and chitinases
    • Merzendorfer, H., and Zimoch, L., Chitin metabolism in insects: structure, function and regulation of chitin synthases and chitinases. J. Exp. Biol., 206, 4393-4412 (2003).
    • (2003) J. Exp. Biol. , vol.206 , pp. 4393-4412
    • Merzendorfer, H.1    Zimoch, L.2
  • 5
    • 0005351839 scopus 로고
    • Characterization and evolution of chitinolytic enzymes in lower vertebrates
    • Jeuniaux, C., Dandrifosse, G., and Micha, J. C., Characterization and evolution of chitinolytic enzymes in lower vertebrates. Biochem. Syst. Ecol., 10, 365-372 (1982).
    • (1982) Biochem. Syst. Ecol. , vol.10 , pp. 365-372
    • Jeuniaux, C.1    Dandrifosse, G.2    Micha, J.C.3
  • 7
    • 0001773321 scopus 로고    scopus 로고
    • The ever-widening diversity of chitinase
    • Gooday, G. W., The ever-widening diversity of chitinase. Carbohydr. Eur., 19, 18-22 (1997).
    • (1997) Carbohydr. Eur. , vol.19 , pp. 18-22
    • Gooday, G.W.1
  • 8
    • 0033208853 scopus 로고    scopus 로고
    • Chitinase in whole and glandular human salivas and in whole saliva of patients with periodontal inflammation
    • van Steijn, G. J., Nieuw Amerongen, A. V., Veerman, E. C. I., Kasanmoentalib, S., and Overdijk, B., Chitinase in whole and glandular human salivas and in whole saliva of patients with periodontal inflammation. Eur. J. Oral Sci., 107, 328-337 (1999).
    • (1999) Eur. J. Oral Sci. , vol.107 , pp. 328-337
    • Van Steijn, G.J.1    Nieuw Amerongen, A.V.2    Veerman, E.C.I.3    Kasanmoentalib, S.4    Overdijk, B.5
  • 9
    • 0009006860 scopus 로고    scopus 로고
    • Aggressive and defensive roles for chitinases
    • eds. Jolles, P., and Muzzarelli, R. A. A., Birkhauser-Verlag, Basel
    • Gooday, G. W., Aggressive and defensive roles for chitinases. In "Chitin and Chitinases", eds. Jolles, P., and Muzzarelli, R. A. A., Birkhauser-Verlag, Basel, pp. 156-169 (1999).
    • (1999) Chitin and Chitinases , pp. 156-169
    • Gooday, G.W.1
  • 10
    • 0001545557 scopus 로고
    • Insect endochitinases: Glycoproteins from moulting fluid, integument and pupal haemolymph of Manduca sexta L.
    • Koga, D., Jilka, J., and Kramer, K. J., Insect endochitinases: glycoproteins from moulting fluid, integument and pupal haemolymph of Manduca sexta L. Insect Biochem., 13, 295-305 (1983).
    • (1983) Insect Biochem. , vol.13 , pp. 295-305
    • Koga, D.1    Jilka, J.2    Kramer, K.J.3
  • 11
    • 0001080202 scopus 로고
    • Appearance of chitinolytic enzymes in integument of Bombyx mori during the larval-pupal transformation: Evidence for zymogenic forms
    • Koga, D., Fujimoto, H., Funakoshi, T., Utsumi, T., and Ide, A., Appearance of chitinolytic enzymes in integument of Bombyx mori during the larval-pupal transformation: evidence for zymogenic forms. Insect Biochem., 19, 123-128 (1989).
    • (1989) Insect Biochem. , vol.19 , pp. 123-128
    • Koga, D.1    Fujimoto, H.2    Funakoshi, T.3    Utsumi, T.4    Ide, A.5
  • 12
    • 0000112152 scopus 로고
    • Effects of 20-hydroxyecdysone and KK-42 on chitinase and β-N-acetylglucosaminidase during the larval-pupal transformation of Bombyx mori
    • Koga, D., Funakoshi, T., Fujimoto, H., Kuwano, E., Eto, M., and Ide, A., Effects of 20-hydroxyecdysone and KK-42 on chitinase and β-N- acetylglucosaminidase during the larval-pupal transformation of Bombyx mori. Insect Biochem., 21, 277-284 (1991).
    • (1991) Insect Biochem. , vol.21 , pp. 277-284
    • Koga, D.1    Funakoshi, T.2    Fujimoto, H.3    Kuwano, E.4    Eto, M.5    Ide, A.6
  • 13
    • 0000114650 scopus 로고
    • Immunoblot analysis of chitinolytic enzymes in integument and molting fluid of the silkworm, Bombyx mori, and the tobacco hornworm, Manduca sexta
    • Koga, D., Funakoshi, T., Mizuki, K., Ide, A., Kramer, K. J., Zen, K. C., Choi, H., and Muthukrishnan, S., Immunoblot analysis of chitinolytic enzymes in integument and molting fluid of the silkworm, Bombyx mori, and the tobacco hornworm, Manduca sexta. Insect Biochem. Mol. Biol., 22, 305-311 (1992).
    • (1992) Insect Biochem. Mol. Biol. , vol.22 , pp. 305-311
    • Koga, D.1    Funakoshi, T.2    Mizuki, K.3    Ide, A.4    Kramer, K.J.5    Zen, K.C.6    Choi, H.7    Muthukrishnan, S.8
  • 14
    • 0036891089 scopus 로고    scopus 로고
    • Presence of chitinase and beta-N-acetylglucosaminidase in the Aedes aegypti: A chitinolytic system involving peritrophic matrix formation and degradation
    • Filho, B. P. D., Lemos, F. J. A., Secundino, N. F. C., Pascoa, V., Pereira, S. T., and Pimenta, P. F. P., Presence of chitinase and beta-N-acetylglucosaminidase in the Aedes aegypti: a chitinolytic system involving peritrophic matrix formation and degradation. Insect Biochem. Mol. Biol., 32, 1723-1729 (2002).
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1723-1729
    • Filho, B.P.D.1    Lemos, F.J.A.2    Secundino, N.F.C.3    Pascoa, V.4    Pereira, S.T.5    Pimenta, P.F.P.6
  • 15
    • 0042168237 scopus 로고    scopus 로고
    • Comparative biochemistry of insect and plant chitinases
    • eds. Muzzarelli., R. A. A., Atec-Edizioni., Senigallia, Italy
    • Koga, D., Comparative biochemistry of insect and plant chitinases. In "Chitin Enzymology Vol. 2", eds. Muzzarelli., R. A. A., Atec-Edizioni., Senigallia, Italy, pp. 85-94 (1996).
    • (1996) Chitin Enzymology Vol. 2 , vol.2 , pp. 85-94
    • Koga, D.1
  • 16
    • 0031417776 scopus 로고    scopus 로고
    • Induced resistance in plants and the role of pathogenesis-related proteins
    • van Loon, L. C., Induced resistance in plants and the role of pathogenesis-related proteins. Eur. J. Plant Pathol., 103, 753-765 (1997).
    • (1997) Eur. J. Plant Pathol. , vol.103 , pp. 753-765
    • Van Loon, L.C.1
  • 17
    • 0024897575 scopus 로고
    • Induced plant response to herbivory
    • Karban, R., and Myers, J. H., Induced plant response to herbivory. Annu. Rev. Ecol. Syst., 20, 331-348 (1989).
    • (1989) Annu. Rev. Ecol. Syst. , vol.20 , pp. 331-348
    • Karban, R.1    Myers, J.H.2
  • 18
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 19
    • 0033288885 scopus 로고    scopus 로고
    • Biochemistry of chitinases
    • eds. Jolles, P., and Muzzarelli, R. A. A., Birkhauser Publishing, Basel
    • Koga, D., Mitsustomi, M., Kono, M., and Matsumiya, M., Biochemistry of chitinases. In "Chitin and Chitinases", eds. Jolles, P., and Muzzarelli, R. A. A., Birkhauser Publishing, Basel, pp. 111-123 (1999).
    • (1999) Chitin and Chitinases , pp. 111-123
    • Koga, D.1    Mitsustomi, M.2    Kono, M.3    Matsumiya, M.4
  • 20
    • 0027297246 scopus 로고
    • Chitinases of fungi and plants: Their involvement in morphogenesis and host-parasite interaction
    • Sahai, A. S., and Manocha, M. S., Chitinases of fungi and plants: their involvement in morphogenesis and host-parasite interaction. FEMS Microbiol. Rev., 11, 317-338 (1993).
    • (1993) FEMS Microbiol. Rev. , vol.11 , pp. 317-338
    • Sahai, A.S.1    Manocha, M.S.2
  • 22
    • 0029071185 scopus 로고
    • The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 Å resolution
    • Hart, P. J., Pfluger, H. D., Monzingo, A. F., Hollis, T., and Robertus, J. D., The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 Å resolution. J. Mol. Biol., 248, 402-413 (1995).
    • (1995) J. Mol. Biol. , vol.248 , pp. 402-413
    • Hart, P.J.1    Pfluger, H.D.2    Monzingo, A.F.3    Hollis, T.4    Robertus, J.D.5
  • 23
    • 0028316274 scopus 로고
    • Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12
    • Armand, S., Tomita, H., Heyraud, A., Gey, C., Watanabe, T., and Henrissat, B., Stereochemical course of the hydrolysis reaction catalyzed by chitinases A1 and D from Bacillus circulans WL-12. FEBS Lett., 343, 177-180 (1994).
    • (1994) FEBS Lett. , vol.343 , pp. 177-180
    • Armand, S.1    Tomita, H.2    Heyraud, A.3    Gey, C.4    Watanabe, T.5    Henrissat, B.6
  • 24
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate-assisted catalysis
    • Terwisscha van Scheltinga, A. C., Armand, S., Kalk, K. H., Isogai, A., Henrissat, B., and Dijkstra, B. W., Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate-assisted catalysis. Biochem., 34, 15619-15623 (1995).
    • (1995) Biochem. , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 25
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott, M. L., Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev., 90, 1171-1202 (1990).
    • (1990) Chem. Rev. , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 26
    • 0001616015 scopus 로고
    • Comparative biochemistry of chitinases-anomeric form of the reaction products
    • Fukamizo, T., Koga, D., and Goto, S., Comparative biochemistry of chitinases-anomeric form of the reaction products. Biosci. Biotechnol. Biochem., 59, 311-313 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 311-313
    • Fukamizo, T.1    Koga, D.2    Goto, S.3
  • 27
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G., and Henrissat, B., Structures and mechanisms of glycosyl hydrolases. Structure, 3, 853-859 (1995).
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 29
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and Bairoch, A., New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 30
    • 0028774705 scopus 로고
    • Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Terwisscha van Scheltinga, A. C., Halk, K. H., Beintema, J. J., and Dijkstra, B. W., Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure, 2, 1181-1189 (1994).
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Terwisscha Van Scheltinga, A.C.1    Halk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 31
    • 0014475358 scopus 로고
    • The stereospecificity of human, hen, and papaya lysozymes
    • Dahlquist, F. W., Borders, C. L., Jacobson, G., and Raftery, M. A., The stereospecificity of human, hen, and papaya lysozymes. Biochem., 8, 694-700 (1969).
    • (1969) Biochem. , vol.8 , pp. 694-700
    • Dahlquist, F.W.1    Borders, C.L.2    Jacobson, G.3    Raftery, M.A.4
  • 33
    • 0020145803 scopus 로고
    • Purification and characterization of chitinase from the stable fly, Stomoxys calcitrans
    • Chen, A. C., Mayer, R. T., and De Loach, J. R., Purification and characterization of chitinase from the stable fly, Stomoxys calcitrans. Arch. Biochem. Biophys., 216, 314-321 (1982).
    • (1982) Arch. Biochem. Biophys. , vol.216 , pp. 314-321
    • Chen, A.C.1    Mayer, R.T.2    De Loach, J.R.3
  • 35
    • 0035957749 scopus 로고    scopus 로고
    • Cloning and functional expression of a chitinase cDNA from the common cutworm, Spodoptera litura, using a recombinant baculovirus lacking the virus-encoded chitinase gene
    • Shinoda, T., Kobayashi, J., Matsui, M., and Chinzei, Y., Cloning and functional expression of a chitinase cDNA from the common cutworm, Spodoptera litura, using a recombinant baculovirus lacking the virus-encoded chitinase gene. Insect Biochem. Mol. Biol., 31, 521-532 (2001).
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 521-532
    • Shinoda, T.1    Kobayashi, J.2    Matsui, M.3    Chinzei, Y.4
  • 36
    • 0036504060 scopus 로고    scopus 로고
    • Purification and characterization of chitinase from pupae of Pieris rapae Boisduval
    • Kondo, K., Matsumoto, M., Kojo, A., and Maeda, R., Purification and characterization of chitinase from pupae of Pieris rapae Boisduval. J. Chem. Eng. Japan, 35, 241-246 (2002).
    • (2002) J. Chem. Eng. Japan , vol.35 , pp. 241-246
    • Kondo, K.1    Matsumoto, M.2    Kojo, A.3    Maeda, R.4
  • 37
    • 0037106454 scopus 로고    scopus 로고
    • A novel putative insect chitinase with multiple catalytic domains: Hormonal regulation during metamorphosis
    • Royer, V., Fraichard, S., and Bouhin, H., A novel putative insect chitinase with multiple catalytic domains: hormonal regulation during metamorphosis. Biochem. J., 366, 921-928 (2002).
    • (2002) Biochem. J. , vol.366 , pp. 921-928
    • Royer, V.1    Fraichard, S.2    Bouhin, H.3
  • 38
    • 0037354808 scopus 로고    scopus 로고
    • Temporal, spatial and induced expression of chitinase in the spruce budworm, Choristoneura fumiferana
    • Zheng, Y.-P., Retnakaran, A., Krell, P. J., Arif, B. M., Primavera, M., and Feng, Q.-L., Temporal, spatial and induced expression of chitinase in the spruce budworm, Choristoneura fumiferana. J. Insect Physiol., 49, 241-247 (2003).
    • (2003) J. Insect Physiol. , vol.49 , pp. 241-247
    • Zheng, Y.-P.1    Retnakaran, A.2    Krell, P.J.3    Arif, B.M.4    Primavera, M.5    Feng, Q.-L.6
  • 39
    • 0141625701 scopus 로고    scopus 로고
    • Molecular characterization of chitinase from polyphagous pest Helicoverpa armigera
    • Ahmad, T., Rajagopal, R., and Bhatnagar, R. K., Molecular characterization of chitinase from polyphagous pest Helicoverpa armigera. Biochem. Biophys. Res. Commun., 310, 188-195 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 188-195
    • Ahmad, T.1    Rajagopal, R.2    Bhatnagar, R.K.3
  • 40
    • 0030665155 scopus 로고    scopus 로고
    • Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae
    • Shen, Z. C., and Jacobs-Lorena, M., Characterization of a novel gut-specific chitinase gene from the human malaria vector Anopheles gambiae. J. Biol. Chem., 272, 28895-28900 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 28895-28900
    • Shen, Z.C.1    Jacobs-Lorena, M.2
  • 41
    • 0242711342 scopus 로고    scopus 로고
    • Chitinolytic activities in the gut of Aedes aegypti (Diptera: Culicidae) larva in their role in digestion of chitin-rich structures
    • Souza-Neto, J. A., Gusmao, D. S., and Lemos, F. J. A., Chitinolytic activities in the gut of Aedes aegypti (Diptera: Culicidae) larva in their role in digestion of chitin-rich structures. Com. Biochem. Physiol., A136, 717-724 (2003).
    • (2003) Com. Biochem. Physiol. , vol.A136 , pp. 717-724
    • Souza-Neto, J.A.1    Gusmao, D.S.2    Lemos, F.J.A.3
  • 42
    • 0033288815 scopus 로고    scopus 로고
    • Chitinases of human parasites and their implications as antiparasitic targets
    • Shahabuddin, M., and Vinetz, J. M., Chitinases of human parasites and their implications as antiparasitic targets. EXS., 87, 223-234 (1999).
    • (1999) EXS , vol.87 , pp. 223-234
    • Shahabuddin, M.1    Vinetz, J.M.2
  • 43
    • 0034616295 scopus 로고    scopus 로고
    • Chitinases of the avian malarial parsite Plasmodeum gallinaceum, a class of enzymes necessary for parasitic invasion of the mosquito midgut
    • Vinetz, J. M., Valenzuela, J. G., Specht, C. A., Aravind, L., Langer, R. C., Ribeiro, J. M. C., and Kaslow, D. C., Chitinases of the avian malarial parsite Plasmodeum gallinaceum, a class of enzymes necessary for parasitic invasion of the mosquito midgut. J. Biol. Chem., 275, 10331-10341 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 10331-10341
    • Vinetz, J.M.1    Valenzuela, J.G.2    Specht, C.A.3    Aravind, L.4    Langer, R.C.5    Ribeiro, J.M.C.6    Kaslow, D.C.7
  • 44
    • 0026565262 scopus 로고
    • Transmission-blocking antibodies recognize microfilarial chitinase in brugian filariasis
    • Fuhrman, J. A., Lane, W. S., Smith, R. F., Plessens, W. F., and Perler, F. B., Transmission-blocking antibodies recognize microfilarial chitinase in brugian filariasis. Proc. Natl. Acad. Sci. U.S.A., 89, 1548-1552 (1992).
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 1548-1552
    • Fuhrman, J.A.1    Lane, W.S.2    Smith, R.F.3    Plessens, W.F.4    Perler, F.B.5
  • 45
    • 0032570604 scopus 로고    scopus 로고
    • The Ld Cht1 gene encodes the secretory chitinase of the human pathogen Leishmania donovani
    • Shakarian, A. M., and Dwyer, D. M., The Ld Cht1 gene encodes the secretory chitinase of the human pathogen Leishmania donovani. Gene, 208, 315-322 (1998).
    • (1998) Gene , vol.208 , pp. 315-322
    • Shakarian, A.M.1    Dwyer, D.M.2
  • 46
    • 0030756551 scopus 로고    scopus 로고
    • A novel role for the peritrophic matrix in protecting Leishmania from the hydrolytic activities of the sand fly midgut
    • Pimenta, P. F. P., Modi, G. B., Pereira, S. T., Shahabuddin, M., and Sacks, D. L., A novel role for the peritrophic matrix in protecting Leishmania from the hydrolytic activities of the sand fly midgut. Parasitology, 115, 359-369 (1997).
    • (1997) Parasitology , vol.115 , pp. 359-369
    • Pimenta, P.F.P.1    Modi, G.B.2    Pereira, S.T.3    Shahabuddin, M.4    Sacks, D.L.5
  • 47
    • 0142092482 scopus 로고    scopus 로고
    • The peritrophic matrix limits the rate of digestion in adult Anopheles stephensi and Aedes aegypti mosquitoes
    • Villalon, J. M., Ghosh, A., and Jacobs-Lorena, M., The peritrophic matrix limits the rate of digestion in adult Anopheles stephensi and Aedes aegypti mosquitoes. J. Insect Physiol., 49, 891-895 (2003).
    • (2003) J. Insect Physiol. , vol.49 , pp. 891-895
    • Villalon, J.M.1    Ghosh, A.2    Jacobs-Lorena, M.3
  • 48
    • 0002884412 scopus 로고    scopus 로고
    • Ultrastructural and cytochemical characterization of aphid invasion by the hyphomycete Verticillium lecanii
    • Askary, H., Benhamou, N., and Brodeur, J., Ultrastructural and cytochemical characterization of aphid invasion by the hyphomycete Verticillium lecanii. J. Inv. Pathol., 74, 1-13 (1999).
    • (1999) J. Inv. Pathol. , vol.74 , pp. 1-13
    • Askary, H.1    Benhamou, N.2    Brodeur, J.3
  • 49
    • 0027348936 scopus 로고
    • Chitin synthesis and degradation as targets for pesticide action
    • Cohen, E., Chitin synthesis and degradation as targets for pesticide action. Arch. Biochem. Physiol., 22, 245-261 (1993).
    • (1993) Arch. Biochem. Physiol. , vol.22 , pp. 245-261
    • Cohen, E.1
  • 50
    • 0344110241 scopus 로고    scopus 로고
    • Insect chitinases: Molecular biology and potential use as biopesticides
    • Kramer, K. J., and Muthukrishnan, S., Insect chitinases: molecular biology and potential use as biopesticides. Insect Biochem. Mol. Biol., 27, 887-900 (1997).
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 887-900
    • Kramer, K.J.1    Muthukrishnan, S.2
  • 51
    • 31444456022 scopus 로고    scopus 로고
    • Effect of Bombyx mori chitinase against Japanese pine sawyer (Monochamus alternatus) adult as a biopesticide
    • Kabir, K. E., Sugimoto, H., Tado, H., Endo, K., Yamanaka, A., Tanaka, S., and Koga, D., Effect of Bombyx mori chitinase against Japanese pine sawyer (Monochamus alternatus) adult as a biopesticide. Biosci. Biotechnol. Biochem., 70, 219-229 (2006).
    • (2006) Biosci. Biotechnol. Biochem. , vol.70 , pp. 219-229
    • Kabir, K.E.1    Sugimoto, H.2    Tado, H.3    Endo, K.4    Yamanaka, A.5    Tanaka, S.6    Koga, D.7
  • 52
    • 0019883721 scopus 로고
    • A convenient synthesis of glycolchitin, a substrate of lysozyme
    • Yamada, H., and Imoto, T., A convenient synthesis of glycolchitin, a substrate of lysozyme. Carbohyd. Res., 92, 160-162 (1981).
    • (1981) Carbohyd. Res. , vol.92 , pp. 160-162
    • Yamada, H.1    Imoto, T.2
  • 54
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T., and Yagishita, K., A simple activity measurement of lysozyme. Agric. Biol. Chem., 35, 1154-1156 (1971).
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 55
    • 37049156324 scopus 로고
    • Universal buffer solutions and the dissociation constant of veronal
    • Britton, H. T. S., and Robinson, R. A., Universal buffer solutions and the dissociation constant of veronal. J. Chem. Soc., 1931, 1456-1462 (1931).
    • (1931) J. Chem. Soc. , vol.1931 , pp. 1456-1462
    • Britton, H.T.S.1    Robinson, R.A.2
  • 56
    • 0001199167 scopus 로고    scopus 로고
    • HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme
    • Koga, D., Yoshioka, T., and Arakane, Y., HPLC analysis of anomeric formation and cleavage pattern by chitinolytic enzyme. Biosci. Biotechnol. Biochem., 62, 1643-1646 (1998).
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1643-1646
    • Koga, D.1    Yoshioka, T.2    Arakane, Y.3
  • 57
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 58
    • 0035109098 scopus 로고    scopus 로고
    • A genomic clone for a chitinase gene from the silkworm, Bombyx mori: Structural organization identifies functional motifs
    • Abdel-Banat, B. M., and Koga, D., A genomic clone for a chitinase gene from the silkworm, Bombyx mori: structural organization identifies functional motifs. Insect Biohem. Mol. Biol., 31, 497-508 (2001).
    • (2001) Insect Biohem. Mol. Biol. , vol.31 , pp. 497-508
    • Abdel-Banat, B.M.1    Koga, D.2
  • 59
    • 0037163120 scopus 로고    scopus 로고
    • Alternative splicing of the primary transcript generates heterogeneity within the products of the gene for Bombyx mori chitinase
    • Abdel-Banat, B. M., and Koga, D., Alternative splicing of the primary transcript generates heterogeneity within the products of the gene for Bombyx mori chitinase. J. Biol. Chem., 277, 30524-30534 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 30524-30534
    • Abdel-Banat, B.M.1    Koga, D.2
  • 60
    • 0036561022 scopus 로고    scopus 로고
    • Analysis of hydrolytic activity of a 65-kDa chitinase from the silkworm, Bombyx mori
    • Abdel-Banat, B. M., Zhou, W., Karasuda, S., and Koga, D., Analysis of hydrolytic activity of a 65-kDa chitinase from the silkworm, Bombyx mori. Biosci. Biotechnol. Biochem., 66, 1119-1122 (2002).
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1119-1122
    • Abdel-Banat, B.M.1    Zhou, W.2    Karasuda, S.3    Koga, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.