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Recombinant expression and characterization of N-acetylglucosaminyltransferase I derived from Nicotiana tabacum

Paper ID Volume ID Publish Year Pages File Format Full-Text
21359 43218 2010 4 PDF Available
Title
Recombinant expression and characterization of N-acetylglucosaminyltransferase I derived from Nicotiana tabacum
Abstract

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.

Keywords
Acetylglucosaminyltransferase; Tobacco; Glycosylation; Characterization; Substrate specificity
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Recombinant expression and characterization of N-acetylglucosaminyltransferase I derived from Nicotiana tabacum
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 109, Issue 4, April 2010, Pages 388–391
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us