Immobilized liposome chromatography for refolding and purification of protein.
J Chromatogr B Biomed Sci Appl
; 743(1-2): 93-9, 2000 Jun 23.
Article
en En
| MEDLINE
| ID: mdl-10942276
Small unilamellar liposomes were utilized as a kind of aqueous two-phase system and artificial chaperone which specifically recognize protein conformation with fluctuated structure. Liposomes showed highly selective binding ability to conformationally changed proteins treated with various concentrations of guanidinium hydrochloride, as evaluated by immobilized liposome chromatography (ILC). In refolding of proteins, liposomes bound to refolding intermediate of proteins and prevented them from forming intermolecular aggregates. Refolding of bovine carbonic anhydrase, lysozyme and ribonuclease A was significantly improved in the presence of liposomes. Furthermore, by utilizing ILC, refolding of proteins was also successfully and simply carried out with considerable high reactivation yield.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Cromatografía Liquida
Límite:
Animals
Idioma:
En
Revista:
J Chromatogr B Biomed Sci Appl
Asunto de la revista:
QUIMICA CLINICA
Año:
2000
Tipo del documento:
Article
País de afiliación:
Japón
Pais de publicación:
Países Bajos