E. coli-based production of recombinant HMG-17 and its antibacterial domain / 生物医学工程学杂志
Journal of Biomedical Engineering
;
(6): 773-777, 2005.
Article
in Chinese
| WPRIM
| ID: wpr-238344
ABSTRACT
Total RNA was extracted from human LAK cell, and a cDNA encoding mature peptide HMG-17 and its alpha helix domain was amplified by RT-PCR. The recombinant prokaryotic expression vector pGEX-1lambdaT-HMG-17 and pGEX-1lambdaT HMG-17alpha helix was constructed. Using affinity chromatography, thrombin cleaving and AU-PAGE elution, we obtained the purified HMG-17. Analyses of MIC, MEC and MBC indicated that HMG-17 and HMG-17alpha had strong antibacterial activity. MIC of the alpha-helic domain was almost the same as that of HMG17, suggesting that the alpha-helic structure would be essential for the antibacterial activity of HMG-17.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Peptides
/
Pharmacology
/
Prokaryotic Cells
/
Recombinant Proteins
/
Killer Cells, Lymphokine-Activated
/
Chemistry
/
HMGN2 Protein
/
Escherichia coli
/
Genetics
/
Metabolism
Limits:
Humans
Language:
Chinese
Journal:
Journal of Biomedical Engineering
Year:
2005
Type:
Article
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