Cloning and fusion expression of the antimicrobial peptide thanatin gene in Escherichia coli

Cloning and fusion expression of the antimicrobial peptide thanatin gene in Escherichia coli

The thanatin gene was obtained and inserted into expression vector pGEX-3X by a DNA recombinant method which was checked by nucleotide sequencing. The fusion protein of GST-thanatin was produced by IPTG induction in Escherichia coli (BL21). The expression level was about 20%. The fusion protein was...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:K'un ch'ung hsueh pao 2003-01, Vol.46 (1), p.114-117
Hauptverfasser: Weng, Hong-Biao, Niu, Bao-Long, Meng, Zhi-Qi, Xu, Meng-Kui
Format: Artikel
Sprache:chi
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:The thanatin gene was obtained and inserted into expression vector pGEX-3X by a DNA recombinant method which was checked by nucleotide sequencing. The fusion protein of GST-thanatin was produced by IPTG induction in Escherichia coli (BL21). The expression level was about 20%. The fusion protein was purified by GST affinity chromatography and digested by enterokinase. Partly purified with Sephadex G-25, the final product, thanatin exhibited antimicrobial activity.
ISSN:0454-6296