The purification of HBV full-length PreS protein in Pichia pastoris / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 708-712, 2005.
Article
Dans Chinois
| WPRIM
| ID: wpr-237086
ABSTRACT
The Pichia pastoris strain GS115-PreS could produce a high expression level of full-length PreS protein that secreted to the supernatant after methanol induction in the fermentation. The Western blot analysis showed a single band with expected molecular mass of 48kD and that the major component of the particles was the full-length PreS protein (PreS1 + PreS2 + S) and small envelope protein (S) of 48 and 28 kD, respectively. Electron microscopy image showed PreS particles with 30 nm in diameter. The supernatants of the fermentation were desalted and concentrated. Purified PreS protein was obtained by DEAE-SFF anion exchange column chromatography and the PreS particles were obtained by ultracentrifugation and sucrose density gradient. The ELISA assay results proved that both full-length PreS protein and particles showed high immunogenicity and specificity. P/N ratio further demonstrated that the immunogenicity of the particles is higher than the full-length PreS protein.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Pichia
/
Précurseurs de protéines
/
Protéines recombinantes
/
Protéines de l'enveloppe virale
/
Virus de l'hépatite B
/
Allergie et immunologie
/
Génétique
/
Antigènes de surface du virus de l'hépatite B
/
Métabolisme
Limites du sujet:
Humains
langue:
Chinois
Texte intégral:
Chinese Journal of Biotechnology
Année:
2005
Type:
Article
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