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  • 2000-2004  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Identification of the cellulose-binding and the cell wall-binding domains of Eubacterium cellulosolvens 5 cellulose-binding protein A (CBPA) (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 214 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The cellulose-binding domain (CBD) and the cell wall-binding domain (CWBD) of Eubacterium cellulosolvens 5 cellulose-binding protein A (CBPA) have been determined. The gene (cbpA) encoding CBPA and its derivatives were expressed in Escherichia coli. We were able to obtain the eight recombinant proteins and examine for their cellulose-binding ability, cell wall-binding ability and carboxymethyl cellulase (CMCase) activity. Since five recombinant proteins, which contain the unknown domain (UD-2) located between two linker-like regions of CBPA, bound to cellulose, this region has been identified as the CBD. The CBD did not show a significant sequence similarity with any other CBDs. Moreover, the N-terminal region of CBPA showed a significant sequence similarity with a catalytic domain of glycosyl hydrolase family 9, and the recombinant proteins containing the region showed CMCase activity. Since the UD-3, which is located in the C-terminal region of CBPA, bound to the cell walls of E. cellulosolvens 5, the region has been identified as the CWBD. However, the CWBD did not show a significant sequence similarity with any other proteins previously reported.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11333.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning, nucleotide sequence and expression of the gene encoding the cellulose-binding protein A (CBPA) of Eubacterium cellulosolvens 5 (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 207 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The nucleotide sequence of the gene encoding the cellulose-binding protein A (CBPA) of Eubacterium cellulosolvens 5 was determined. The gene consists of an open reading frame of 3453 nucleotides and encodes a protein of 1151 amino acids with a molecular mass of 126 408 Da. The deduced amino acid sequence of CBPA contained one domain highly similar to a catalytic domain of glycosyl hydrolases belonging to family 9, two linker-like domains and four domains of unknown function. Among the four domains of unknown function, the domains 1 and 2 region had significant homology in amino acid sequence with the cellulose-binding domains in the family 9 glycosyl hydrolases. The cloned gene was inserted into an expression vector, pBAD-TOPO, and expressed in Escherichia coli as a fused protein. The fused protein was detected by immunoblotting using antiserum against CBPA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11042.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of the cellulose-binding domain of Fibrobacter succinogenes endoglucanase F (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 183 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The cellulose-binding domain (CBD) of Fibrobacter succinogenes endoglucanase F (EGF) has been determined. The gene encoding EGF (celF) and its derivatives were expressed in Escherichia coli. We were able to obtain eight recombinant proteins and examine their cellulose-binding ability and endoglucanase activity. Because four recombinant proteins, which contain the first N-terminal reiterated region of EGF, bound to cellulose, the region has been identified as the CBD. Although the CBD did not show significant sequence similarity with any other CBDs, it did show significant similarity with a part of endoglucanase J (CelJ) of Clostridium thermocellum F1. Moreover, a large part of the C-terminal catalytic region of EGF showed sequence similarity with α-L-arabinofuranosidases of glycosyl hydrolase family 51.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb08940.x
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    Paper (German National Licenses)
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