|Title: ||CEL1: a novel cellulose binding protein secreted by Agaricus bisporus during growth on crystalline cellulose.|
|Citation: ||FEMS Microbiology Letters, 116(3): 293-299|
|Publisher: ||Blackwell Publishing|
|Issue Date: ||1994 |
|PubMed ID: ||8181702|
|Additional Links: ||http://www3.interscience.wiley.com/journal/119276698/abstract|
|Submitted date: ||2007-01-24|
|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.|
|Description: ||Metadata only|
|Keywords: ||Agaricus bisporus|
|Appears in Collections: ||Molecular Pharmacology Research Group|
|Files in This Item:|
There are no files associated with this item.
All Items in WIRE are protected by copyright, with all rights reserved, unless otherwise indicated.