[Purification of recombinant proteins with an example of tumor necrosis factor thymosin-alpha1].
Prikl Biokhim Mikrobiol
; 46(2): 243-7, 2010.
Article
en Ru
| MEDLINE
| ID: mdl-20391771
ABSTRACT
Hybrid protein, cancer necrosis factor thymosin-alpha1 (CNF-T), when synthesizing in strain-producer of Escherichia coli SG200-50 with plasmid pThy315, was a part of "inclusion bodies" mostly in the form of a high-molecular complex with other proteins due to the S-S bonds formation. An approach of purification of CNF-T has been proposed, which is based on the destruction of the complex in the presence of sodium dodecylsulfate (DDS-NA) and dithiotreitol (DDT) followed by gel-filtration on Sephadex G-100 and renaturation by ultrafiltration on hollow fibers. The method allows the isolation of electrophoretically homogeneous CNF-T containing no DDS-Na and having high cytotoxic activity against cancer cells of mouse adenocarcinome L-929. The yield of CNF-T achieved 80% relative its content in biomass and 30% relative the total protein.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Timosina
/
Proteínas Recombinantes
/
Cromatografía en Gel
Límite:
Animals
Idioma:
Ru
Revista:
Prikl Biokhim Mikrobiol
Año:
2010
Tipo del documento:
Article