Construction of novel thioredoxin fusion protein expression system and the production of recombinant Lf-CATH2 / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 403-410, 2015.
Article
in Chinese
| WPRIM
| ID: wpr-240633
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.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Thioredoxins
/
Recombinant Fusion Proteins
/
Chromatography, Affinity
/
Escherichia coli
/
Cathelicidins
/
Genetic Vectors
/
Genetics
Language:
Chinese
Journal:
Chinese Journal of Biotechnology
Year:
2015
Type:
Article
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