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    CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.

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    Authors
    Armesilla, Angel cc
    Thurston, Christopher F.
    Yague, Ernesto
    Issue Date
    1994
    Submitted date
    2007-01-24
    
    Metadata
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    Abstract
    The cel1 gene of Agaricus bisporus encodes a protein (CEL1) that has an architecture resembling the multi-domain fungal cellulases, although the sequence of its putative catalytic core is not matched by any other in the protein and nucleic acid data bases. The N-terminal half of the putative catalytic domain of CEL1 was expressed in Escherichia coli as a fusion protein with glutathione-S-transferase. The fusion protein was used to raise a CEL1-specific antibody. CEL1 was detected as an extracellular 49.8 kDa protein in A. bisporus cellulose-grown cultures, where it bound strongly to cellulose. CEL1 was neither an endoglucanase, a cellobiohydrolase able to hydrolyze fluorogenic cellobiosides, a beta-glucosidase, a xylanase, nor a cellobiose: quinone oxidoreductase. CEL1 was present in some fractions of culture fluid separated by electrophoresis which released soluble sugars from crystalline cellulose.
    Citation
    FEMS Microbiology Letters, 116(3): 293-299
    Publisher
    Blackwell Publishing
    URI
    http://hdl.handle.net/2436/7745
    DOI
    10.1111/j.1574-6968.1994.tb06718.x
    PubMed ID
    8181702
    Additional Links
    http://www3.interscience.wiley.com/journal/119276698/abstract
    Type
    Journal article
    Language
    en
    Description
    Metadata only
    ISSN
    0378-1097
    ae974a485f413a2113503eed53cd6c53
    10.1111/j.1574-6968.1994.tb06718.x
    Scopus Count
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    Research Institute in Healthcare Science

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