Overexpression of HIV-1 P17 protein in Escherichia coli and its purification / 吉林大学学报(医学版)
Journal of Jilin University(Medicine Edition)
;
(6): 19-21, 2001.
Artículo
en Chino
| WPRIM
| ID: wpr-411581
ABSTRACT
Objective:
To highly express HIV-1p17 in E.coli and purify the protein.Methods:
①Recombinant plasmid was constructed by inserting HIV-1p17 gene amplified by PCR into plasmid vector,pET28c;②The recombinant plasmid was expressed in BL21,BL21(DE3),BL21(DE3) plysS and HMS174(DE3) of E.coli separately;③The target protein were purified with Ni-NTA resin;④The purified protein was detected by western blot and ELISA.Results:
The expression of the P17 protein in BL21(DE3) represented up to 32% of total protein in E.coli,which was the most amounts compared with other kinds of E.coli.The purity of the purified protein reached 95%.The purified protein was recognized by HIV-1P17McAb as well as by HIV-1 positive serum.Conclusion:
The recombinant plasmid is highly expressed in BL21(DE3) of E.coli that can be proceeded to the immunocompetence and the bioactivity research.The method of Ni-NTA resin is simple with low protein losing and high purity.And the purified p17 can be employed in early detection of HIV-1 infection and prediction of the clinical progression.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Tipo de estudio:
Estudio de tamizaje
Idioma:
Chino
Revista:
Journal of Jilin University(Medicine Edition)
Año:
2001
Tipo del documento:
Artículo
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