Overexpression and Purification of p24 and gp41 Proteins of Human Immunodeficiency Virus Type 1 in E. coli
Journal of the Korean Society of Virology
;
: 21-30, 1998.
Article
in Korean
| WPRIM
| ID: wpr-70606
ABSTRACT
Synthetic genes encoding the gag p24 and the part of the envelope protein gp41 of the human immunodeficiency virus (HIV-1) were cloned and overexpressed as fusion proteins in Escherichia coli, using an expression vector carrying 77 promoter and the poly-histidine leader sequence. The overexpressed p24 fusion protein was purified by centrifugation, Ni-affinity chromatography and CM-sepharose chromatography The overexpressed gp41 fusion protein was purified by centrifugation, C4 chromatography and DEAE-sepharose chromatography. The purified fusion proteins showed a high level of purity and immunoreactivity in SDS-polyacrylamide gel electrophoresis and western blot analysis. These results suggest that this prokaryotic expression-purification method is suitable for obtaining a large amount of the viral antigen which may be useful for screening of antibodies to HIV-1 in human blood samples.
Full text:
Available
Index:
WPRIM (Western Pacific)
Main subject:
Centrifugation
/
Mass Screening
/
Blotting, Western
/
Chromatography
/
HIV-1
/
HIV
/
Clone Cells
/
Electrophoresis
/
Escherichia coli
/
Genes, Synthetic
Type of study:
Screening study
Limits:
Humans
Language:
Korean
Journal:
Journal of the Korean Society of Virology
Year:
1998
Type:
Article
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