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
en Ko
| WPRIM
| ID: wpr-70606
Biblioteca responsable:
WPRO
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.
Texto completo:
1
Índice:
WPRIM
Asunto principal:
Centrifugación
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Tamizaje Masivo
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Western Blotting
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Cromatografía
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VIH-1
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VIH
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Células Clonales
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Electroforesis
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Escherichia coli
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Genes Sintéticos
Tipo de estudio:
Screening_studies
Límite:
Humans
Idioma:
Ko
Revista:
Journal of the Korean Society of Virology
Año:
1998
Tipo del documento:
Article