title: [E. coli-based production of recombinant HMG-17 and its antibacterial domain].
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.
authors.affiliation: Research Unit of Infection & Immunity, West China Medical Center of Sichuan University, Chengdu 610041, China.
authors.forename: Yun
authors.initials: Y
authors.lastname: Feng
authors.forename: Huarong
authors.initials: H
authors.lastname: Yang
authors.lastname: Huangning
authors.forename: Qi
authors.initials: Q
authors.lastname: Wu
authors.forename: Lang
authors.initials: L
authors.lastname: Bao
authors.forename: Boyao
authors.initials: B
authors.lastname: Wang
mesh_terms: D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D024242:HMGN2 Protein / Q000096:biosynthesis* / Q000235:genetics / Q000494:pharmacology*; D006801:Humans; D015979:Killer Cells, Lymphokine-Activated / Q000737:chemistry; D010455:Peptides / Q000235:genetics / Q000494:pharmacology; D011387:Prokaryotic Cells / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D024242:HMGN2 Protein; D010455:Peptides; D011994:Recombinant Proteins