Journal of Bioscience and Bioengineering 2010-Apr
Recombinant expression and characterization of N-acetylglucosaminyltransferase I derived from Nicotiana tabacum.
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The C-terminal catalytic domain of tobacco N-acetylglucosaminyltransferase I fused to maltose-binding protein was produced in Escherichia coli as a soluble form with significant activity. The protein was affinity-purified using amylose resin, and its enzymatic properties were investigated, including its divalent cation requirements, optimal temperature, optimal pH, and substrate specificity.