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  • 2000-2004  (2)
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  • 1
    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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  • 2
    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
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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