期刊
BIOTECHNOLOGY LETTERS
卷 30, 期 4, 页码 671-676出版社
SPRINGER
DOI: 10.1007/s10529-007-9588-y
关键词
carbohydrate; expression; Photobacterium damsela; sialic acid; sialyltransferase
资金
- NIGMS NIH HHS [R01GM076360, R01 GM076360, R01 GM076360-03] Funding Source: Medline
Photobacterium damsela alpha 2,6-sialyltransferase was cloned as N- and C- His-tagged fusion proteins with different lengths (16-497 aa or 113-497 aa). Expression and activity assays indicated that the N-terminal 112 amino acid residues of the protein were not required for its alpha 2,6-sialyltransferase activity. Among four truncated forms tested, N-His-tagged Delta 15Pd2,6ST(N) containing 16-497 amino acid residues had the highest expression level. Similar to the Delta 15Pd2,6ST(N), the shorter Delta 112Pd2,6ST(N) was active in a wide pH range of 7.5-10.0. A divalent metal ion was not required for the sialyltransferase activity, and the addition of EDTA and dithiothreitol did not affect the activity significantly.
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