[Construction of novel thioredoxin fusion protein expression system and the production of recombinant Lf-CATH2].
Sheng Wu Gong Cheng Xue Bao
; 31(3): 403-10, 2015 Mar.
Article
en Zh
| MEDLINE
| ID: mdl-26204761
ABSTRACT
The objective of this study was to construct an improved thioredoxin fusion protein expression system, and express the cathelicidin-derived peptide, Lf-CATH2. The improved fusion vector Lf-CATH2-pET32α(-TS) was successfully constructed by firstly deleting the thrombin site and S tag from the pET-32α vector, then inserting the Lf-CATH2 plus a thrombin site instead. Afterwards, Lf-CATH2 was expressed in Escherichia coli as fusion protein. After the cleavage by thrombin, Lf-CATH2 was released and subsequently separated using affinity chromatography. The antimicrobial activity of purified Lf-CATH2 was also examined. The improved expression vector significantly increased enzyme cleavage efficiency by 37%, and Lf-CATH2 could be expressed in high yield and maintain the biological activity. This novel thioredoxin fusion protein expression system enables a quick production of high-yield bioactive cationic peptides like cathelicidins.
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Bases de datos:
MEDLINE
Asunto principal:
Tiorredoxinas
/
Proteínas Recombinantes de Fusión
/
Catelicidinas
/
Vectores Genéticos
Idioma:
Zh
Revista:
Sheng Wu Gong Cheng Xue Bao
Asunto de la revista:
BIOTECNOLOGIA
Año:
2015
Tipo del documento:
Article