메뉴 건너뛰기




Volumn 20, Issue 2, 1997, Pages 143-149

Comparison of the adsorption properties of a single-chain antibody fragment fused to a fungal or bacterial cellulose-binding domain

Author keywords

Cellulose; Cellulose binding domain; Fusion protein; Immobilization; Single chain antibody

Indexed keywords

ANTIBODIES; BACTERIA; BINDING ENERGY; CELLULOSE; ENZYME IMMOBILIZATION; FUNGI; PROTEINS;

EID: 0031081624     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00109-3     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 0028088841 scopus 로고
    • The biological degradation of cellulose
    • 1. Béguin, P. and Aubert, J.-P. The biological degradation of cellulose. FEMS Microbiol. Rev. 1994, 13, 25-58
    • (1994) FEMS Microbiol. Rev. , vol.13 , pp. 25-58
    • Béguin, P.1    Aubert, J.-P.2
  • 2
    • 0025804758 scopus 로고
    • Domains in microbial-1,4-glycanases: Sequence conservation, function and enzyme families
    • 2. Gilkes, N. R., Henrissat, B., Kilburn, D. G., Miller, R. C. Jr., and Warren, R. A. J. Domains in microbial-1,4-glycanases: Sequence conservation, function and enzyme families. Microbiol. Rev. 1991, 55, 303-315
    • (1991) Microbiol. Rev. , vol.55 , pp. 303-315
    • Gilkes, N.R.1    Henrissat, B.2    Kilburn, D.G.3    Miller R.C., Jr.4    Warren, R.A.J.5
  • 3
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • 3. Henrissat, B. and Bairoch, A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 1993, 293, 781-788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 5
    • 0024962351 scopus 로고
    • Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing
    • 5. Kraulis, P. J., Clore, G. M., Nilges, M., Jones, T. A., Pettersson, G., Knowles, J., and Gronenborn, A. M. Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing. Biochemistry 1989, 28, 7241-7257
    • (1989) Biochemistry , vol.28 , pp. 7241-7257
    • Kraulis, P.J.1    Clore, G.M.2    Nilges, M.3    Jones, T.A.4    Pettersson, G.5    Knowles, J.6    Gronenborn, A.M.7
  • 7
    • 0029119131 scopus 로고
    • The difference in affinity between two fungal cellulosebinding domains is dominated by a single amino acid substitution
    • 7. Linder, M., Lindeberg, G., Reinikainen, T., Teeri, T. T., and Pettersson, G. The difference in affinity between two fungal cellulosebinding domains is dominated by a single amino acid substitution. FEBS Lett. 1995, 372, 96-98
    • (1995) FEBS Lett. , vol.372 , pp. 96-98
    • Linder, M.1    Lindeberg, G.2    Reinikainen, T.3    Teeri, T.T.4    Pettersson, G.5
  • 9
    • 0028364450 scopus 로고
    • The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: Evidence for involvement of tryptophan residues in binding
    • 9. Din, N., Forsythe, I. J., Burtnick, L. D., Gilkes, N. R., Miller, R. C., Warren, R. A. J., and Kilburn, D. G. The cellulose-binding domain of endoglucanase A (CenA) from Cellulomonas fimi: Evidence for involvement of tryptophan residues in binding. Mol. Microb. 1994, 11, 747-755
    • (1994) Mol. Microb. , vol.11 , pp. 747-755
    • Din, N.1    Forsythe, I.J.2    Burtnick, L.D.3    Gilkes, N.R.4    Miller, R.C.5    Warren, R.A.J.6    Kilburn, D.G.7
  • 10
    • 0027386771 scopus 로고
    • The role of conserved tryptophan residues in the interaction of a bacterial cellulose-binding domain with its ligand
    • 10. Poole, D. M., Hazlewood, G. P., Huskisson, N. S., Virden, R., and Gilbert, H. J. The role of conserved tryptophan residues in the interaction of a bacterial cellulose-binding domain with its ligand. FEMS Microbiol. Lett. 1993, 106, 77-84
    • (1993) FEMS Microbiol. Lett. , vol.106 , pp. 77-84
    • Poole, D.M.1    Hazlewood, G.P.2    Huskisson, N.S.3    Virden, R.4    Gilbert, H.J.5
  • 11
    • 45149144143 scopus 로고
    • Isolated fungal cellulase terminal domains and a synthetic minimum analogue bind to cellulose
    • 11. Johansson, G., Ståhlberg, G., Lindeberg, G., Engström, Å., and Pettersson, G. Isolated fungal cellulase terminal domains and a synthetic minimum analogue bind to cellulose. FEBS Lett. 1989, 243, 389-393
    • (1989) FEBS Lett. , vol.243 , pp. 389-393
    • Johansson, G.1    Ståhlberg, G.2    Lindeberg, G.3    Engström, A.4    Pettersson, G.5
  • 12
    • 0027909736 scopus 로고
    • Cex) of an exoglucanase from Cellulomonas fimi. Production in Escherichia coli and characterization of the polypeptide
    • Cex) of an exoglucanase from Cellulomonas fimi. Production in Escherichia coli and characterization of the polypeptide. Biotechnol. Bioeng. 1993a, 42, 401-409
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 401-409
    • Ong, E.1    Gilkes, N.R.2    Miller R.C., Jr.3    Warren, R.A.J.4
  • 14
    • 0026503034 scopus 로고
    • The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats
    • 14. Coutinho, J. B., Gilkes, N. R., Warren, R. A. J., Kilburn, D. G., and Miller, R. C., Jr. The binding of Cellulomonas fimi endoglucanase C (CenC) to cellulose and Sephadex is mediated by the N-terminal repeats. Mol. Microb. 1992, 6, 1243-1252
    • (1992) Mol. Microb. , vol.6 , pp. 1243-1252
    • Coutinho, J.B.1    Gilkes, N.R.2    Warren, R.A.J.3    Kilburn, D.G.4    Miller R.C., Jr.5
  • 15
    • 0026349480 scopus 로고
    • Non-hydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase
    • 15. Din, N., Gilkes, N. R., Tekant, B., Miller, R. C. Jr., Warren, R. A. J., and Kilburn, D. G. Non-hydrolytic disruption of cellulose fibres by the binding domain of a bacterial cellulase. Bio/Technology 1991, 9, 1096-1099
    • (1991) Bio/Technology , vol.9 , pp. 1096-1099
    • Din, N.1    Gilkes, N.R.2    Tekant, B.3    Miller R.C., Jr.4    Warren, R.A.J.5    Kilburn, D.G.6
  • 16
    • 0027503664 scopus 로고
    • Production and properties of a factor X-cellulose-binding domain fusion protein
    • 16. Assouline, Z., Shen, H., Kilburn, D. G., and Warren, R. A. J. Production and properties of a factor X-cellulose-binding domain fusion protein. Prot. Eng. 1993, 6, 787-792
    • (1993) Prot. Eng. , vol.6 , pp. 787-792
    • Assouline, Z.1    Shen, H.2    Kilburn, D.G.3    Warren, R.A.J.4
  • 17
    • 0029278707 scopus 로고
    • Purification of human interleukin-2 using the cellulose-binding domain of a prokaryotic cellulase
    • 17. Ong, E., Alimonti, J. B., Greenwood, J. M., Miller, R. C. Jr., Warren, R. A. J., and Kilburn, D. G. Purification of human interleukin-2 using the cellulose-binding domain of a prokaryotic cellulase. Bioseparation 1995, 5, 95-104
    • (1995) Bioseparation , vol.5 , pp. 95-104
    • Ong, E.1    Alimonti, J.B.2    Greenwood, J.M.3    Miller R.C., Jr.4    Warren, R.A.J.5    Kilburn, D.G.6
  • 19
    • 0002239657 scopus 로고
    • Cellulose binding domains: Properties and applications
    • (Suominen, P. and Reinikainen, T., Eds.). Foundation for Biotechnical and Industrial Fermentation Research, Helsinki
    • 19. Kilburn, D. G., Assouline, Z., Din, N., Gilkes, N. R., Ong, E., Tomme, P., and Warren, R. A. J. Cellulose binding domains: Properties and applications. In: Proc. 2nd Tricel Symp. Trichoderma reesei Celluloses Hydrolases (Suominen, P. and Reinikainen, T., Eds.). Foundation for Biotechnical and Industrial Fermentation Research, Helsinki, 1993a, 281-290
    • (1993) Proc. 2nd Tricel Symp. Trichoderma Reesei Celluloses Hydrolases , pp. 281-290
    • Kilburn, D.G.1    Assouline, Z.2    Din, N.3    Gilkes, N.R.4    Ong, E.5    Tomme, P.6    Warren, R.A.J.7
  • 21
    • 0028206082 scopus 로고
    • A streptavidin-cellulose-binding domain fusion protein that binds biotinylated proteins to cellulose
    • 21. Le, K., Gilkes, N. R., Kilburn, D. G., Miller, R. C. Jr., Saddler, J. N., and Warren, R. A. J. A streptavidin-cellulose-binding domain fusion protein that binds biotinylated proteins to cellulose. Enzyme Microb. Technol. 1994, 16, 496-500
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 496-500
    • Le, K.1    Gilkes, N.R.2    Kilburn, D.G.3    Miller R.C., Jr.4    Saddler, J.N.5    Warren, R.A.J.6
  • 22
    • 0024355972 scopus 로고
    • Enzyme immobilisation with the cellulose-binding domain of a Cellulomonas fimi exoglucanase
    • 22. Ong, E., Gilkes, N. R., Miller, R. C. Jr., Warren, R. A. J., and Kilburn, D. G. Enzyme immobilisation with the cellulose-binding domain of a Cellulomonas fimi exoglucanase. Bio/Technology 1989, 7, 604-607
    • (1989) Bio/Technology , vol.7 , pp. 604-607
    • Ong, E.1    Gilkes, N.R.2    Miller R.C., Jr.3    Warren, R.A.J.4    Kilburn, D.G.5
  • 23
    • 0026011001 scopus 로고
    • Enzyme immobilisation using a cellulose-binding domain: Properties of a glucosidase fusion protein
    • 23. Ong, E., Gilkes, N. R., Miller, R. C. Jr., and Warren, R. A. J. Enzyme immobilisation using a cellulose-binding domain: Properties of a glucosidase fusion protein. Enzyme Microb. Technol. 1991, 13, 59-65
    • (1991) Enzyme Microb. Technol. , vol.13 , pp. 59-65
    • Ong, E.1    Gilkes, N.R.2    Miller R.C., Jr.3    Warren, R.A.J.4
  • 26
    • 0001190823 scopus 로고
    • Occurrence of cellulases in enzyme preparations from microorganisms
    • 26. Walseth, C. S. Occurrence of cellulases in enzyme preparations from microorganisms. Tappi 1952, 35, 228-233
    • (1952) Tappi , vol.35 , pp. 228-233
    • Walseth, C.S.1
  • 27
    • 0023372652 scopus 로고
    • Construction of cDNA libraries by blunt end ligation: High-frequency cloning of long cDNAs from filamentous fungi
    • 27. Teeri, T. T., Kumar, V., Lehtovaara, P., and Knowles, J. K. C. Construction of cDNA libraries by blunt end ligation: High-frequency cloning of long cDNAs from filamentous fungi. Anal. Biochem. 1987, 164, 60-67
    • (1987) Anal. Biochem. , vol.164 , pp. 60-67
    • Teeri, T.T.1    Kumar, V.2    Lehtovaara, P.3    Knowles, J.K.C.4
  • 32
    • 0026425806 scopus 로고
    • Integrated fluid handling system for biomolecular interaction analysis
    • 32. Sjölander, S. and Urbanicky, C. Integrated fluid handling system for biomolecular interaction analysis. Anal. Chem. 1991, 63, 2338-2345
    • (1991) Anal. Chem. , vol.63 , pp. 2338-2345
    • Sjölander, S.1    Urbanicky, C.2
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 33. 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
  • 34
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • 34. Towbin, H., Staehelin, T., and Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 1979, 76, 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 35
    • 0025777266 scopus 로고
    • Monoclonal antibodies against core and cellulose-binding domains of Trichoderma reesei cellobiohydrolase I and II and endoglucanase I
    • 35. Aho, S., Olkkonen, V., Jalava, T., Paloheimo, M., Bühler, R., Niku-Paavola, M. L., Bamford, D. H., and Korhola, M. Monoclonal antibodies against core and cellulose-binding domains of Trichoderma reesei cellobiohydrolase I and II and endoglucanase I. Eur. J. Biochem. 1991, 200, 643-649
    • (1991) Eur. J. Biochem. , vol.200 , pp. 643-649
    • Aho, S.1    Olkkonen, V.2    Jalava, T.3    Paloheimo, M.4    Bühler, R.5    Niku-Paavola, M.L.6    Bamford, D.H.7    Korhola, M.8
  • 36
    • 0025218376 scopus 로고
    • Gel staining techniques
    • 36. Merril, C. R. Gel staining techniques. Methods Enzymol. 1990, 182, 477-478
    • (1990) Methods Enzymol. , vol.182 , pp. 477-478
    • Merril, C.R.1
  • 37
    • 0023410604 scopus 로고
    • Characterisation of the Erwinia carotovora pelB gene and its product pectate lyase
    • 37. Lei, S. P., Lin, H. C., Wang, S. S., Callaway, J. and Wilcox, G. Characterisation of the Erwinia carotovora pelB gene and its product pectate lyase. J. Bacteriol. 1987, 169, 4379-4384
    • (1987) J. Bacteriol. , vol.169 , pp. 4379-4384
    • Lei, S.P.1    Lin, H.C.2    Wang, S.S.3    Callaway, J.4    Wilcox, G.5
  • 38
    • 0027361585 scopus 로고
    • High-level production of an active single-chain Fv fragment in the culture supernatant of Escherichia coli
    • (Cure, J. M. and Lewis, R. E. Jr., Eds.). Karger AG, Basel
    • 38. Sizmann, D., Takkinen, K., Laukkanen, M. L., Saloheimo, M., Candussio, A., Veijola-Bailey, P., and Teeri, T. T. High-level production of an active single-chain Fv fragment in the culture supernatant of Escherichia coli. In: The Year in Immunology Vol. 7 (Cure, J. M. and Lewis, R. E. Jr., Eds.). Karger AG, Basel, 1993, 119-130
    • (1993) The Year in Immunology , vol.7 , pp. 119-130
    • Sizmann, D.1    Takkinen, K.2    Laukkanen, M.L.3    Saloheimo, M.4    Candussio, A.5    Veijola-Bailey, P.6    Teeri, T.T.7
  • 39
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • 39. Karlsson, R., Michaelsson, A., and Mattsson, L. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods 1991, 145, 229-240
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 41
    • 0029144923 scopus 로고
    • Effects of pH and high ionic strength on the adsorption and activity of native and mutated cellobiohydrolase I from Trichoderma reesei
    • 41. Reinikainen, T., Teleman, O., and Teeri, T. T. Effects of pH and high ionic strength on the adsorption and activity of native and mutated cellobiohydrolase I from Trichoderma reesei. Prot. Structure, Function Genet. 1995, 22, 392-403
    • (1995) Prot. Structure, Function Genet. , vol.22 , pp. 392-403
    • Reinikainen, T.1    Teleman, O.2    Teeri, T.T.3
  • 42
    • 0003084197 scopus 로고
    • Recent X-ray crystallographic studies of celluloses
    • (Young, R. A. and Rowell, R. M., Eds.). Wiley Interscience, New York
    • 42. Sarko, A. Recent X-ray crystallographic studies of celluloses. In: Cellulose: Structure, Modification and Hydrolysis (Young, R. A. and Rowell, R. M., Eds.). Wiley Interscience, New York, 1986, 29-66
    • (1986) Cellulose: Structure, Modification and Hydrolysis , pp. 29-66
    • Sarko, A.1
  • 43
    • 0021021887 scopus 로고
    • Adsorption of cellulase from Trichoderma viride on cellulose
    • 43. Ooshima, H., Sakata, M., and Harano, Y. Adsorption of cellulase from Trichoderma viride on cellulose. Biotechnol. Bioeng. 1983, 25, 3103-3114
    • (1983) Biotechnol. Bioeng. , vol.25 , pp. 3103-3114
    • Ooshima, H.1    Sakata, M.2    Harano, Y.3
  • 44
    • 0027968302 scopus 로고
    • The three-dimensional structure of cellobiohydrolase I from Trichoderma reesei reveals a lysozyme-like active site on a lectin-like framework
    • 44. Divne, C., Ståhlberg, J., Reinikainen, T., Ruohonen, L., Pettersson, G., Knowles, J. K. C., Teeri, T. T., and Jones, T. A. The three-dimensional structure of cellobiohydrolase I from Trichoderma reesei reveals a lysozyme-like active site on a lectin-like framework. Science 1994, 265, 524-528
    • (1994) Science , vol.265 , pp. 524-528
    • Divne, C.1    Ståhlberg, J.2    Reinikainen, T.3    Ruohonen, L.4    Pettersson, G.5    Knowles, J.K.C.6    Teeri, T.T.7    Jones, T.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.