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Volumn 1, Issue 4, 2012, Pages 338-347

Biochemical, structural and functional characterization of two novel antifungal endoglucanases from Anabaena laxa

Author keywords

Antifungal activity; Cyanobacteria; Endoglucanase; Site directed mutagenesis; TLC

Indexed keywords

ANABAENA; ANABAENA LAXA; CYANOBACTERIA;

EID: 84866360333     PISSN: 18788181     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcab.2012.08.001     Document Type: Article
Times cited : (16)

References (58)
  • 1
    • 0037415334 scopus 로고    scopus 로고
    • Positional expression effects of cysteine mutations in the Thermobifida fusca cellulase Cel6A and Cel6B catalytic domains
    • Ai Y.C., Zhang S., Wilson D.B. Positional expression effects of cysteine mutations in the Thermobifida fusca cellulase Cel6A and Cel6B catalytic domains. Enzyme Microb. Technol. 2003, 32:331-336.
    • (2003) Enzyme Microb. Technol. , vol.32 , pp. 331-336
    • Ai, Y.C.1    Zhang, S.2    Wilson, D.B.3
  • 2
    • 84966143176 scopus 로고
    • Enzymatic treatment of clover root hairs removes a barrier to Rhizobium host specificity
    • Al-Mallah M.K., Davey M.R., Cooking E.C. Enzymatic treatment of clover root hairs removes a barrier to Rhizobium host specificity. Biotechnology 1987, 5:1319-1322.
    • (1987) Biotechnology , vol.5 , pp. 1319-1322
    • Al-Mallah, M.K.1    Davey, M.R.2    Cooking, E.C.3
  • 6
  • 7
    • 79952742069 scopus 로고    scopus 로고
    • Hydrolysis of cellulose in synergistic mixtures of Β-glucosidase and endo/exocellulase Cel9A from Thermobifida fusca
    • Chir J.L., Wan C.F., Chou C.H., Wu A.T. Hydrolysis of cellulose in synergistic mixtures of Β-glucosidase and endo/exocellulase Cel9A from Thermobifida fusca. Biotechnol. Lett. 2011, 33:777-782.
    • (2011) Biotechnol. Lett. , vol.33 , pp. 777-782
    • Chir, J.L.1    Wan, C.F.2    Chou, C.H.3    Wu, A.T.4
  • 9
    • 0032539533 scopus 로고    scopus 로고
    • Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A° and its cellobiose complex at 2.0 A° resolution
    • Davies G.J., Dauter M., Brzozowski A.M., Bjornvad M.E., Andersen K.V., Schulein M. Structure of the Bacillus agaradherans family 5 endoglucanase at 1.6 A° and its cellobiose complex at 2.0 A° resolution. Biochemistry 1998, 17:1926-1932.
    • (1998) Biochemistry , vol.17 , pp. 1926-1932
    • Davies, G.J.1    Dauter, M.2    Brzozowski, A.M.3    Bjornvad, M.E.4    Andersen, K.V.5    Schulein, M.6
  • 10
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano W.L., Ultsch M.H., de Vos A.M., Wells J.A. Convergent solutions to binding at a protein-protein interface. Science 2000, 287:1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    de Vos, A.M.3    Wells, J.A.4
  • 12
    • 77953285162 scopus 로고    scopus 로고
    • Partial purification and characterisation of endoglucanase from an edible mushroom, Lepista flaccid
    • Elvan H., Ertunga N.S., Yildirim M., Colak A. Partial purification and characterisation of endoglucanase from an edible mushroom, Lepista flaccid. Food Chem. 2010, 123:291-295.
    • (2010) Food Chem. , vol.123 , pp. 291-295
    • Elvan, H.1    Ertunga, N.S.2    Yildirim, M.3    Colak, A.4
  • 13
    • 37549021020 scopus 로고    scopus 로고
    • Purification and characterization of a novel endo-Β-1, 4-glucanase from the thermoacidophilic Aspergillus terreus
    • Gao J., Weng H., Xi Y., Zhu D., Han S. Purification and characterization of a novel endo-Β-1, 4-glucanase from the thermoacidophilic Aspergillus terreus. Biotechnol. Lett. 2008, 30:323-327.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 323-327
    • Gao, J.1    Weng, H.2    Xi, Y.3    Zhu, D.4    Han, S.5
  • 14
    • 84871559853 scopus 로고    scopus 로고
    • Purification and characterization of a novel antifungal endo-type chitosanase from Anabaena fertilissima
    • Gupta V., Prasanna R., Srivastava A.K., Sharma J. Purification and characterization of a novel antifungal endo-type chitosanase from Anabaena fertilissima. Ann. Microbiol. 2011, 10.1007/s13213-011-0350-2.
    • (2011) Ann. Microbiol.
    • Gupta, V.1    Prasanna, R.2    Srivastava, A.K.3    Sharma, J.4
  • 15
    • 79951554029 scopus 로고    scopus 로고
    • Identification and characterization of endoglucanases for fungicidal activity in Anabaena laxa
    • Gupta V., Natarajan C., Kumar K., Prasanna R. Identification and characterization of endoglucanases for fungicidal activity in Anabaena laxa. J. Appl. Phycol. 2011, 23:73-81.
    • (2011) J. Appl. Phycol. , vol.23 , pp. 73-81
    • Gupta, V.1    Natarajan, C.2    Kumar, K.3    Prasanna, R.4
  • 16
    • 77951532673 scopus 로고    scopus 로고
    • Identification, characterization and regulation of a novel antifungal chitosanase gene (cho) in Anabaena sp
    • Gupta V., Prasanna R., Natarajan C., Srivastava A.K., Sharma J. Identification, characterization and regulation of a novel antifungal chitosanase gene (cho) in Anabaena sp. Appl. Environ. Microbiol. 2010, 76:2769-2777.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2769-2777
    • Gupta, V.1    Prasanna, R.2    Natarajan, C.3    Srivastava, A.K.4    Sharma, J.5
  • 17
    • 0000521463 scopus 로고
    • Characterization of a bifunctional cellulase and its structural gene
    • Han S.J., Yoo Y.J., Kang H.S. Characterization of a bifunctional cellulase and its structural gene. J. Biol. Chem. 1995, 270:26012-26019.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26012-26019
    • Han, S.J.1    Yoo, Y.J.2    Kang, H.S.3
  • 18
    • 0037616181 scopus 로고    scopus 로고
    • Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: mechanistic implications based on the free and cellobiose-bound forms
    • Hirvonen M., Papageorgiou A.C. Crystal structure of a family 45 endoglucanase from Melanocarpus albomyces: mechanistic implications based on the free and cellobiose-bound forms. J. Mol. Biol. 2003, 329:403-410.
    • (2003) J. Mol. Biol. , vol.329 , pp. 403-410
    • Hirvonen, M.1    Papageorgiou, A.C.2
  • 19
    • 43749115333 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of a novel endoglucanase (CMCase) from Gymnoascella citrina produced under solid-state condition
    • Jabbar A., Rashid M.H., Javed M.R., Perveen R., Malana M.A. Kinetics and thermodynamics of a novel endoglucanase (CMCase) from Gymnoascella citrina produced under solid-state condition. J. Ind. Microbiol. Biotechnol. 2008, 35:515-524.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 515-524
    • Jabbar, A.1    Rashid, M.H.2    Javed, M.R.3    Perveen, R.4    Malana, M.A.5
  • 20
    • 33745901081 scopus 로고    scopus 로고
    • Conformation and microenvironment of the active site of a low molecular weight 1,4-Β-d-glucan glucanohydrolase from an alkalothermophilic Thermomonospora sp.: involvement of lysine and cysteine residues
    • Jagtap S., Rao M. Conformation and microenvironment of the active site of a low molecular weight 1,4-Β-d-glucan glucanohydrolase from an alkalothermophilic Thermomonospora sp.: involvement of lysine and cysteine residues. Biochem. Biophys. Res. Commun. 2006, 347:428-432.
    • (2006) Biochem. Biophys. Res. Commun. , vol.347 , pp. 428-432
    • Jagtap, S.1    Rao, M.2
  • 21
    • 70450250730 scopus 로고    scopus 로고
    • Fast PCR software for PCR primer and probe design and repeat search
    • Kalendar R., Lee D., Schulman A.H. Fast PCR software for PCR primer and probe design and repeat search. Gene. Gene. Gene. 2009, 3:1-14.
    • (2009) Gene. Gene. Gene. , vol.3 , pp. 1-14
    • Kalendar, R.1    Lee, D.2    Schulman, A.H.3
  • 23
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: a case study using the Phyre server
    • Kelley L.A., Sternberg M.J.E. Protein structure prediction on the web: a case study using the Phyre server. Nat. Protoc. 2009, 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 24
    • 38049060254 scopus 로고    scopus 로고
    • A proteomic strategy to discover Β-glucosidases from Aspergillus fumigatus with two-dimensional page in-gel activity assay and tandem mass spectrometry
    • Kim K.H., Brown K.M., Harris P.V., Langston J.A., Cherry J.R. A proteomic strategy to discover Β-glucosidases from Aspergillus fumigatus with two-dimensional page in-gel activity assay and tandem mass spectrometry. J. Proteome Res. 2007, 6:4749-4757.
    • (2007) J. Proteome Res. , vol.6 , pp. 4749-4757
    • Kim, K.H.1    Brown, K.M.2    Harris, P.V.3    Langston, J.A.4    Cherry, J.R.5
  • 26
  • 27
    • 46949111816 scopus 로고    scopus 로고
    • Purification and characterization of a new family 45 endoglucanase, STCE1, from Staphylotrichum coccosporum and its overproduction in Humicola insolens
    • Koga J., Baba Y., Shimonaka A., Nishimura T., Hanamura S., Kono T. Purification and characterization of a new family 45 endoglucanase, STCE1, from Staphylotrichum coccosporum and its overproduction in Humicola insolens. Appl. Microbiol. Biotechnol. 2008, 74:4210-4217.
    • (2008) Appl. Microbiol. Biotechnol. , vol.74 , pp. 4210-4217
    • Koga, J.1    Baba, Y.2    Shimonaka, A.3    Nishimura, T.4    Hanamura, S.5    Kono, T.6
  • 28
    • 60249099179 scopus 로고    scopus 로고
    • Purification and biochemical characterization of carboxymethyl cellulase (CMCase) from a catabolite repression insensitive mutant of Bacillus pumilus
    • Kotchoni S.O., Gachomo E.W., Omafuvbe B.O., Shonukan O.O. Purification and biochemical characterization of carboxymethyl cellulase (CMCase) from a catabolite repression insensitive mutant of Bacillus pumilus. Int. J. Agric. Biol. 2006, 8:286-292.
    • (2006) Int. J. Agric. Biol. , vol.8 , pp. 286-292
    • Kotchoni, S.O.1    Gachomo, E.W.2    Omafuvbe, B.O.3    Shonukan, O.O.4
  • 29
    • 0025438921 scopus 로고
    • Purification and characterisation of two endoglucanases from Arthrobotrys oligospora
    • Kumble K.D., Trivedi P.N., Jaffar M.B. Purification and characterisation of two endoglucanases from Arthrobotrys oligospora. Indian J. Biochem. Biophys. 1990, 27:146-150.
    • (1990) Indian J. Biochem. Biophys. , vol.27 , pp. 146-150
    • Kumble, K.D.1    Trivedi, P.N.2    Jaffar, M.B.3
  • 30
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 25444481552 scopus 로고    scopus 로고
    • Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion
    • Larsson A.M., Bergfors T., Dultz E., Irwin D.C., Roos A., Driguez H., Wilson D.B., Jones T.A. Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion. Biochemistry 2005, 44:12915-12922.
    • (2005) Biochemistry , vol.44 , pp. 12915-12922
    • Larsson, A.M.1    Bergfors, T.2    Dultz, E.3    Irwin, D.C.4    Roos, A.5    Driguez, H.6    Wilson, D.B.7    Jones, T.A.8
  • 33
    • 0035139051 scopus 로고    scopus 로고
    • Production, purification and properties of an endoglucanase produced by the hyphomycete Chalara (Syn. Thielaviopsis) paradoxa CH32
    • Lucas R., Robles A., Garcia M.T., Alvarez De Cienfuegos G., Galvez A. Production, purification and properties of an endoglucanase produced by the hyphomycete Chalara (Syn. Thielaviopsis) paradoxa CH32. J. Agric. Food. Chem. 2001, 49:79-85.
    • (2001) J. Agric. Food. Chem. , vol.49 , pp. 79-85
    • Lucas, R.1    Robles, A.2    Garcia, M.T.3    Alvarez De Cienfuegos, G.4    Galvez, A.5
  • 35
    • 77951730348 scopus 로고    scopus 로고
    • Biocontrol potential of cyanobacterial metabolites against damping off disease caused by Pythium aphanidermatum in solanaceous vegetables
    • Manjunath M., Prasanna R., Lata, D.P., Singh R., Kumar A., Jaggi S., Kaushik B.D. Biocontrol potential of cyanobacterial metabolites against damping off disease caused by Pythium aphanidermatum in solanaceous vegetables. Arch. Phytopathol. Plant Protect. 2010, 43:666-677.
    • (2010) Arch. Phytopathol. Plant Protect. , vol.43 , pp. 666-677
    • Manjunath, M.1    Prasanna, R.2    Lata, D.P.3    Singh, R.4    Kumar, A.5    Jaggi, S.6    Kaushik, B.D.7
  • 36
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 37
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity
    • Morrissey J.H. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Chem. 1981, 117:307-310.
    • (1981) Anal. Chem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 38
    • 67649231785 scopus 로고    scopus 로고
    • Purification and characterization of an endoglucanase from Aspergillus terreus highly active against barley Β-glucan and xyloglucan
    • Nazir A., Soni R., Saini H.S., Manhas R.K., Chadha B.S. Purification and characterization of an endoglucanase from Aspergillus terreus highly active against barley Β-glucan and xyloglucan. World J. Microbiol. Biotechnol. 2009, 25:1189-1197.
    • (2009) World J. Microbiol. Biotechnol. , vol.25 , pp. 1189-1197
    • Nazir, A.1    Soni, R.2    Saini, H.S.3    Manhas, R.K.4    Chadha, B.S.5
  • 39
    • 0037102477 scopus 로고    scopus 로고
    • Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus
    • Parry N.J., Beever D.E., Owen E., Nerinckx W., Claeyssens M., Van B., Bhat M.K. Biochemical characterization and mode of action of a thermostable endoglucanase purified from Thermoascus aurantiacus. Arch. Biochem. Biophys. 2002, 404:243-253.
    • (2002) Arch. Biochem. Biophys. , vol.404 , pp. 243-253
    • Parry, N.J.1    Beever, D.E.2    Owen, E.3    Nerinckx, W.4    Claeyssens, M.5    Van, B.6    Bhat, M.K.7
  • 40
    • 77951093943 scopus 로고    scopus 로고
    • Bioprospecting for genes involved in the production of chitosanases and microcystin-like compounds in Anabaena strains
    • Prasanna R., Gupta V., Natarajan C., Chaudhary V. Bioprospecting for genes involved in the production of chitosanases and microcystin-like compounds in Anabaena strains. World J. Microbiol. Biotechnol. 2010, 26:717-724.
    • (2010) World J. Microbiol. Biotechnol. , vol.26 , pp. 717-724
    • Prasanna, R.1    Gupta, V.2    Natarajan, C.3    Chaudhary, V.4
  • 42
    • 47649110951 scopus 로고    scopus 로고
    • Evaluation of fungicidal activity of extracellular filtrates of cyanobacteria-possible role of hydrolytic enzymes
    • Prasanna R., Lata N., Tripathi R., Gupta V., Middha S., Joshi M., Ancha R., Kaushik B.D. Evaluation of fungicidal activity of extracellular filtrates of cyanobacteria-possible role of hydrolytic enzymes. J. Basic Microbiol. 2008, 48:186-194.
    • (2008) J. Basic Microbiol. , vol.48 , pp. 186-194
    • Prasanna, R.1    Lata, N.2    Tripathi, R.3    Gupta, V.4    Middha, S.5    Joshi, M.6    Ancha, R.7    Kaushik, B.D.8
  • 44
    • 0029796791 scopus 로고    scopus 로고
    • Structural environment of an essential cysteine residue of xylanase from Chainia sp. (NCL 82.5.1)
    • Rao M., Khadilkar S., Bandivadekar K.R., Deshpande V. Structural environment of an essential cysteine residue of xylanase from Chainia sp. (NCL 82.5.1). Biochem. J. 1996, 316:771-775.
    • (1996) Biochem. J. , vol.316 , pp. 771-775
    • Rao, M.1    Khadilkar, S.2    Bandivadekar, K.R.3    Deshpande, V.4
  • 46
    • 0034731318 scopus 로고    scopus 로고
    • Protein engineering of cellulases
    • Schulein M. Protein engineering of cellulases. Biochim. Biophys. Acta 2000, 1543:239-252.
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 239-252
    • Schulein, M.1
  • 47
    • 0027951683 scopus 로고
    • Ability of Aspergillus niger to tolerate metal ions and minerals in solid state fermentation system for the production of citric acid
    • Shankaranand V.S., Lonsane B. Ability of Aspergillus niger to tolerate metal ions and minerals in solid state fermentation system for the production of citric acid. Process Biochem. 1994, 29:29-39.
    • (1994) Process Biochem. , vol.29 , pp. 29-39
    • Shankaranand, V.S.1    Lonsane, B.2
  • 48
    • 41549164662 scopus 로고    scopus 로고
    • Effect of bipolar membrane electrobasification on chitosanase activity during chitosan hydrolysis
    • Shee F.L.T., Arul J., Brunet S., Bazinet L. Effect of bipolar membrane electrobasification on chitosanase activity during chitosan hydrolysis. J. Biotechnol. 2008, 134:305-311.
    • (2008) J. Biotechnol. , vol.134 , pp. 305-311
    • Shee, F.L.T.1    Arul, J.2    Brunet, S.3    Bazinet, L.4
  • 49
    • 0015076683 scopus 로고
    • Purification and properties of unicellular blue green algae (Order: Chroococcales)
    • Stanier R.Y., Kunisawa R., Mandal M., Cohen-Bazire G. Purification and properties of unicellular blue green algae (Order: Chroococcales). Bacteriol. Rev. 1971, 35:171-305.
    • (1971) Bacteriol. Rev. , vol.35 , pp. 171-305
    • Stanier, R.Y.1    Kunisawa, R.2    Mandal, M.3    Cohen-Bazire, G.4
  • 50
    • 0029856409 scopus 로고    scopus 로고
    • Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group
    • Sulzenbacher G., Driguez H., Henrissat B., Schulein M., Davies G.J. Structure of the Fusarium oxysporum endoglucanase I with a nonhydrolyzable substrate analogue: substrate distortion gives rise to the preferred axial orientation for the leaving group. Biochemistry 1996, 35:15280-15287.
    • (1996) Biochemistry , vol.35 , pp. 15280-15287
    • Sulzenbacher, G.1    Driguez, H.2    Henrissat, B.3    Schulein, M.4    Davies, G.J.5
  • 51
    • 0020032328 scopus 로고
    • Use of congo red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from bovine rumen
    • Teather R.M., Wood P.J. Use of congo red polysaccharide interactions in enumeration and characterization of cellulolytic bacteria from bovine rumen. Appl. Environ. Microbiol. 1982, 43:777-780.
    • (1982) Appl. Environ. Microbiol. , vol.43 , pp. 777-780
    • Teather, R.M.1    Wood, P.J.2
  • 52
    • 0034767214 scopus 로고    scopus 로고
    • Atomic resolution structure of endoglucanase Cel5A in complex with methyl 4, 4II, 4III, 4IV-tetrathio-alpha-cellopentoside highlights the alternative binding modes targeted by substrate mimics
    • Varrot A., Schulein M., Fruchard S., Driguez H., Davies G.J. Atomic resolution structure of endoglucanase Cel5A in complex with methyl 4, 4II, 4III, 4IV-tetrathio-alpha-cellopentoside highlights the alternative binding modes targeted by substrate mimics. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2001, 57:1739-1742.
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.57 , pp. 1739-1742
    • Varrot, A.1    Schulein, M.2    Fruchard, S.3    Driguez, H.4    Davies, G.J.5
  • 53
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe T., Kobori K., Miyashita K., Fujii T., Sakai H., Uchida M., Tanaka H. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 1993, 268:18567-18572.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 54
    • 70350569789 scopus 로고    scopus 로고
    • A new recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4: an extremely thermo-pH-stable esterase
    • Yildirim M., Colak A., Col M., Canakci S. A new recombinant phosphotriesterase homology protein from Geobacillus caldoxylosilyticus TK4: an extremely thermo-pH-stable esterase. Process Biochem. 2009, 44:1366-1373.
    • (2009) Process Biochem. , vol.44 , pp. 1366-1373
    • Yildirim, M.1    Colak, A.2    Col, M.3    Canakci, S.4
  • 55
    • 75249088440 scopus 로고    scopus 로고
    • Roll: a new algorithm for the detection of protein pockets and cavities with a rolling probe sphere
    • Yu J., Zhou Y., Tanaka I., Yao M. Roll: a new algorithm for the detection of protein pockets and cavities with a rolling probe sphere. Bioinformatics 2010, 26:46-52.
    • (2010) Bioinformatics , vol.26 , pp. 46-52
    • Yu, J.1    Zhou, Y.2    Tanaka, I.3    Yao, M.4
  • 56
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies
    • Zor T., Selinger Z. Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal. Biochem. 1996, 236:302-308.
    • (1996) Anal. Biochem. , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2
  • 57
    • 23644445055 scopus 로고    scopus 로고
    • A major new component in the cellulosome of Clostridium thermocellum is a processive endo-Β-1, 4-glucanase producing cellotetraose
    • Zverlov V.V., Schantz N., Schwarz W.H. A major new component in the cellulosome of Clostridium thermocellum is a processive endo-Β-1, 4-glucanase producing cellotetraose. FEMS Microbiol. Lett. 2005, 249:353-358.
    • (2005) FEMS Microbiol. Lett. , vol.249 , pp. 353-358
    • Zverlov, V.V.1    Schantz, N.2    Schwarz, W.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.