Journal
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
Volume 109, Issue 4, Pages 388-391Publisher
SOC BIOSCIENCE BIOENGINEERING JAPAN
DOI: 10.1016/j.jbiosc.2009.10.004
Keywords
Acetylglucosaminyltransferase; Tobacco; Glycosylation; Characterization; Substrate specificity
Funding
- Ministry of Economy, Trade and Industry (METI) of Japan
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) for the Osaka University
Ask authors/readers for more resources
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. (C) 2009, The Society for Biotechnology, Japan. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available
Share Paper
