Construction of recombinant plasmid of Pseudomonas aeruginosa exotoxin A and its secreting expression in E. coli / 解放军医学杂志
Medical Journal of Chinese People's Liberation Army
;
(12)1983.
Article
in Chinese
| WPRIM
| ID: wpr-554662
ABSTRACT
Objective To clone and to express the full-length Pseudomonas aeruginosa exotoxin A gene and to purify the expressed protein using affinity chromatography. Methods Exotoxin A gene was amplified from the recombinant plasmid pSK/PEA-T vector and subcloned into the pMAL-P2X vector. Then the recombinant plasmid pMAL- PEA was transformed to E.coli BL21. After induction with IPTG, the expressed protein was analyzed by SDS-PAGE and purified with affinity chromatography. Results The recombinants expressed the fusion protein at a level of about 20% of total cell proteins, and 80% of the fusion protein was secreted into the supernatant. Conclusion Successful expression and purification of PEA are of significance for in-depth study of the pathogenic mechanism of Pseudomonas aeruginosa and preparing immunotoxin.
Full text:
Available
Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
Medical Journal of Chinese People's Liberation Army
Year:
1983
Type:
Article
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