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Volumn 73, Issue 3, 2007, Pages 675-683

Cellulose digestion by common Japanese freshwater clam Corbicula japonica

Author keywords

Cellulase; Cellulose; Clam; Corbicula japonica; Suspension feeder

Indexed keywords

BIVALVIA; CORBICULA; CORBICULA JAPONICA; HALIOTIDAE; ISOPTERA;

EID: 34250188505     PISSN: 09199268     EISSN: 14442906     Source Type: Journal    
DOI: 10.1111/j.1444-2906.2007.01381.x     Document Type: Article
Times cited : (56)

References (32)
  • 2
    • 0001477510 scopus 로고
    • Cellulase activity and fruit softening in avocado
    • Pesis E, Fuchs Y, Zauberman G. Cellulase activity and fruit softening in avocado. Plant Physiol. 1978 61 : 416 419.
    • (1978) Plant Physiol. , vol.61 , pp. 416-419
    • Pesis, E.1    Fuchs, Y.2    Zauberman, G.3
  • 3
    • 0009426490 scopus 로고
    • Distribution of intestinal bacteria and cellulase activity in harvester termite Trinervitermes-Trinervoides (Nasutitermitinae)
    • Potts RC, Hewitt PH. Distribution of intestinal bacteria and cellulase activity in harvester termite Trinervitermes-Trinervoides (Nasutitermitinae). Insectes Sociaux 1973 20 : 215 220.
    • (1973) Insectes Sociaux , vol.20 , pp. 215-220
    • Potts, R.C.1    Hewitt, P.H.2
  • 4
    • 0015925058 scopus 로고
    • Purification of α-1,4-glucan hydrolase (cellulase) from the snail, Helix pomatia
    • Marshall JJ. Purification of α-1,4-glucan hydrolase (cellulase) from the snail, Helix pomatia. Comp. Biochem. Physiol. B 1973 44 : 981 988.
    • (1973) Comp. Biochem. Physiol. B , vol.44 , pp. 981-988
    • Marshall, J.J.1
  • 8
    • 0034826417 scopus 로고    scopus 로고
    • Cloning and sequencing of a molluscan endo-beta-1,4-glucanase gene from the blue mussel, Mytilus edulis
    • Xu B, Janson JC, Sellos D. Cloning and sequencing of a molluscan endo-beta-1,4-glucanase gene from the blue mussel, Mytilus edulis. Eur. J. Biochem. 2001 268 : 3718 3727.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3718-3727
    • Xu, B.1    Janson, J.C.2    Sellos, D.3
  • 10
    • 0032560853 scopus 로고    scopus 로고
    • A cellulase gene of termite origin
    • Watanabe H, Noda H, Tokuda G, Lo N. A cellulase gene of termite origin. Nature 1998 394 : 330 331.
    • (1998) Nature , vol.394 , pp. 330-331
    • Watanabe, H.1    Noda, H.2    Tokuda, G.3    Lo, N.4
  • 11
    • 17744380000 scopus 로고    scopus 로고
    • Ancient origin of glycosyl hydrolase family 9 cellulase genes
    • Davison A, Blaxter M. Ancient origin of glycosyl hydrolase family 9 cellulase genes. Mol. Biol. Evol. 2005 22 : 1273 1284.
    • (2005) Mol. Biol. Evol. , vol.22 , pp. 1273-1284
    • Davison, A.1    Blaxter, M.2
  • 12
    • 0041926672 scopus 로고    scopus 로고
    • Purification, characterization, cDNA cloning and nucleotide sequencing of a cellulase from the yellow-spotted longicorn beetle, Psacothea hilaris
    • Sugimura M, Watanabe H, Lo N, Saito H. Purification, characterization, cDNA cloning and nucleotide sequencing of a cellulase from the yellow-spotted longicorn beetle, Psacothea hilaris. Eur. J. Biochem. 2003 270 : 3455 3460.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3455-3460
    • Sugimura, M.1    Watanabe, H.2    Lo, N.3    Saito, H.4
  • 13
    • 0037294860 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a cellulase from abalone Haliotis discus hannai
    • Suzuki K, Ojima T, Nishita K. Purification and cDNA cloning of a cellulase from abalone Haliotis discus hannai. Eur. J. Biochem. 2003 270 : 771 778.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 771-778
    • Suzuki, K.1    Ojima, T.2    Nishita, K.3
  • 15
    • 0002110008 scopus 로고
    • Quantitative-analysis of crystalline style carbohydrases in 5 suspension-feeding and deposit-feeding bivalves
    • Brock V, Kennedy VS. Quantitative-analysis of crystalline style carbohydrases in 5 suspension-feeding and deposit-feeding bivalves. J. Exp. Mar. Biol. Ecol. 1992 159 : 51 58.
    • (1992) J. Exp. Mar. Biol. Ecol. , vol.159 , pp. 51-58
    • Brock, V.1    Kennedy, V.S.2
  • 16
    • 0033878935 scopus 로고    scopus 로고
    • Purification, characterization and amino-acid sequence analysis of a thermostable, low molecular mass endo-beta-1,4-glucanase from blue mussel, Mytilus edulis
    • Xu B, Hellman U, Ersson B, Janson JC. Purification, characterization and amino-acid sequence analysis of a thermostable, low molecular mass endo-beta-1,4-glucanase from blue mussel, Mytilus edulis. Eur. J. Biochem. 2000 267 : 4970 4977.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4970-4977
    • Xu, B.1    Hellman, U.2    Ersson, B.3    Janson, J.C.4
  • 19
    • 0002694212 scopus 로고
    • Delta-C-13 measurements as indicators of carbon flow in marine and fresh-water ecosystems
    • Fry B, Sherr EB. Delta-C-13 measurements as indicators of carbon flow in marine and fresh-water ecosystems. Contrib. Mar. Sci. 1984 27 : 13 47.
    • (1984) Contrib. Mar. Sci. , vol.27 , pp. 13-47
    • Fry, B.1    Sherr, E.B.2
  • 20
    • 14744289764 scopus 로고    scopus 로고
    • Utilization of terrestrial organic matter by the bivalve Corbicula japonica estimated from stable isotope analysis
    • Kasai A, Nakata A. Utilization of terrestrial organic matter by the bivalve Corbicula japonica estimated from stable isotope analysis. Fish. Sci. 2005 71 : 151 158.
    • (2005) Fish. Sci. , vol.71 , pp. 151-158
    • Kasai, A.1    Nakata, A.2
  • 21
    • 0020771857 scopus 로고
    • Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas
    • Beguin P. Detection of cellulase activity in polyacrylamide gels using Congo red-stained agar replicas. Anal. Biochem. 1983 131 : 333 336.
    • (1983) Anal. Biochem. , vol.131 , pp. 333-336
    • Beguin, P.1
  • 22
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976 72 : 248 254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0022255318 scopus 로고
    • Determination of reducing sugars in the nanomole range with tetrazolium blue
    • Jue CK, Lipke PN. Determination of reducing sugars in the nanomole range with tetrazolium blue. J. Biochem. Biophys. Methods 1985 11 : 109 115.
    • (1985) J. Biochem. Biophys. Methods , vol.11 , pp. 109-115
    • Jue, C.K.1    Lipke, P.N.2
  • 24
    • 0032733345 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a putative cellulase in the red claw crayfish Cherax quadricarinatus
    • Byrne KA, Lehnert SA, Johnson SE, Moore SS. Isolation of a cDNA encoding a putative cellulase in the red claw crayfish Cherax quadricarinatus. Gene 1999 239 : 317 324.
    • (1999) Gene , vol.239 , pp. 317-324
    • Byrne, K.A.1    Lehnert, S.A.2    Johnson, S.E.3    Moore, S.S.4
  • 25
    • 0030759920 scopus 로고    scopus 로고
    • Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca
    • Sakon J, Irwin D, Wilson DB, Karplus PA. Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca. Nat. Struct. Biol. 1997 4 : 810 818.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 810-818
    • Sakon, J.1    Irwin, D.2    Wilson, D.B.3    Karplus, P.A.4
  • 27
    • 0025866942 scopus 로고
    • Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum
    • Tomme P, Chauvaux S, Beguin P, Millet J, Aubert JP, Claeyssens M. Identification of a histidyl residue in the active center of endoglucanase D from Clostridium thermocellum. J. Biol. Chem. 1991 266 : 10313 10318.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10313-10318
    • Tomme, P.1    Chauvaux, S.2    Beguin, P.3    Millet, J.4    Aubert, J.P.5    Claeyssens, M.6
  • 28
    • 0026643363 scopus 로고
    • Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum
    • Tomme P, van Beeumen J, Claeyssens M. Modification of catalytically important carboxy residues in endoglucanase D from Clostridium thermocellum. Biochem. J. 1992 285 : 319 324.
    • (1992) Biochem. J. , vol.285 , pp. 319-324
    • Tomme, P.1    Van Beeumen, J.2    Claeyssens, M.3
  • 29
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne G. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 1986 14 : 4683 4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 30
    • 0034731387 scopus 로고    scopus 로고
    • The structural basis for the ligand specificity of family 2 carbohydrate-binding modules
    • Simpson PJ, Xie H, Bolam DN, Gilbert HJ, Williamson MP. The structural basis for the ligand specificity of family 2 carbohydrate-binding modules. J. Biol. Chem. 2000 275 : 41137 41142.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41137-41142
    • Simpson, P.J.1    Xie, H.2    Bolam, D.N.3    Gilbert, H.J.4    Williamson, M.P.5
  • 31
    • 0029743877 scopus 로고    scopus 로고
    • The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size
    • Kleman-Leyer KM, Siika-Aho M, Teeri TT, Kirk TK. The cellulases endoglucanase I and cellobiohydrolase II of Trichoderma reesei act synergistically to solubilize native cotton cellulose but not to decrease its molecular size. Appl. Environ. Microbiol. 1996 62 : 2883 2887.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2883-2887
    • Kleman-Leyer, K.M.1    Siika-Aho, M.2    Teeri, T.T.3    Kirk, T.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.