E. coli-based production of recombinant HMG-17 and its antibacterial domain.
- Author:
Yun FENG
1
;
Huarong YANG
;
Huangning
;
Qi WU
;
Lang BAO
;
Boyao WANG
Author Information
1. Research Unit of Infection & Immunity, West China Medical Center of Sichuan University, Chengdu 610041, China.
- Publication Type:Journal Article
- MeSH:
Anti-Bacterial Agents;
biosynthesis;
pharmacology;
Escherichia coli;
genetics;
metabolism;
HMGN2 Protein;
biosynthesis;
genetics;
pharmacology;
Humans;
Killer Cells, Lymphokine-Activated;
chemistry;
Peptides;
genetics;
pharmacology;
Prokaryotic Cells;
metabolism;
Recombinant Proteins;
biosynthesis;
genetics;
pharmacology
- From:
Journal of Biomedical Engineering
2005;22(4):773-777
- CountryChina
- Language:Chinese
-
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.
