
doi: 10.1271/bbb.60.122
pmid: 8824833
A cellulase with activity as a cellobiohydrolase [EC3.2.1.91] was purified from the intestinal juice of the giant snail Achatina fulica. The enzyme (M(r) = about 23,000, and pI = about 5.3) also had a weak beta-glucosidase activity. The amino acid sequence of the N-terminal 20 amino acids was analyzed, and no similarity was noted for sequences of other known cellobiohydrolases.
cellulase, Molecular Sequence Data, Snails, Intestines, Molecular Weight, Cellulase, molluscan cellulase, cellobiohydrolase, Cellulose 1,4-beta-Cellobiosidase, Animals, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, giant snail, Chromatography, High Pressure Liquid
cellulase, Molecular Sequence Data, Snails, Intestines, Molecular Weight, Cellulase, molluscan cellulase, cellobiohydrolase, Cellulose 1,4-beta-Cellobiosidase, Animals, Electrophoresis, Polyacrylamide Gel, Amino Acid Sequence, giant snail, Chromatography, High Pressure Liquid
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