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- W2072197199 abstract "The gene encoding the single cellulose-binding domain II (CBD II) of Clostridium stercorarium xylanase A was fused to the egIV gene encoding endoglucanase IV (EGIV) from Ruminococcus albus . The fusion protein (EGIV + CBDII) expressed in Escherichia coli can be readily purified from the cell-free extract of E. coli in a single step using the affinity of CBD to cellulose. The purified enzyme was cleaved into two moieties, i.e. the catalytic domain and CBD, at a specific site in the linker region by partial digestion with trypsin at 4°C. This result indicates that this CBD belonging to family VI of CBD families can be used as an affinity tag for purification of the recombinant protein." @default.
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- W2072197199 date "1997-01-01" @default.
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- W2072197199 title "Purification of the Ruminococcus albus endoglucanase IV using a cellulose-binding domain as an affinity tag" @default.
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- W2072197199 doi "https://doi.org/10.1016/s0922-338x(97)89259-8" @default.
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