Research of Fusion Expression of Human β-Defensin-3 in Escherichia coli / 中国比较医学杂志
Chinese Journal of Comparative Medicine
;
(6): 670-675, 2007.
Article
Dans Chinois
| WPRIM
| ID: wpr-407569
ABSTRACT
Objective To achieve the fusion expression of the entire human beta-defensin-3(hBD-3) gene. Method We synthesized two oligonucleotide primers accor ding to the codon preference of Escherichia coli. The gene was cloned into p GEX -4T-2 to establish the pGEX-4T-2-hBD-3 as the fusion expression vector by PCR. Transformed into E.coli strain DH5α, the express vector was induced an d ex pressed by IPTG. The fusion protein GST-hBD-3 was obtained by repeated cycles of freezing and thawing, cut by thrombin to attain the recombinant hBD-3 protei n. Result The result of the antibacterial peptide agarose diffu sion assay shows the antibacterial activity of the rhBD-3 against the S.aureu s exists, and it reaches 0.843U. Conclusion The fusion expr ession of the hBD-3 gene is successful.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
langue:
Chinois
Texte intégral:
Chinese Journal of Comparative Medicine
Année:
2007
Type:
Article
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