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High-Level Production of a Novel Antimicrobial Peptide Perinerin in Escherichia coli by Fusion Expression.
- Source :
- Current Microbiology; May2007, Vol. 54 Issue 5, p366-370, 5p
- Publication Year :
- 2007
-
Abstract
- Perinerin is a small antimicrobial peptide (AMP) isolated from an Asian marine clamworm, Perinereis aibuhitensis Grube. It shows marked activity in vitro against both Gram-negative and Gram-positive bacteria. To obtain it in large amounts, the coding sequence of perinerin was cloned into pET32a(+) vector and expression as a Trx fusion protein in Escherichia coli. The soluble fusion protein collected from the supernatant of the cell lyste was separated by Ni<superscript>2+</superscript>-chelating chromatography. The purified protein was then cleaved by Factor Xa protease to release mature perinerin. Final purification was achieved by ion-exchange chromatography. Recombinant perinerin exhibited a similar antimicrobial activity to the native perinerin. These works might provide a significant foundation for the following research on the action of mechanism of marine AMPs. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 03438651
- Volume :
- 54
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Current Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 24990449
- Full Text :
- https://doi.org/10.1007/s00284-006-0466-y