Purification of erythrocyte protein 4.1 by selective interaction with inositol hexaphosphate.
Protein Expr Purif
; 3(6): 488-96, 1992 Dec.
Article
en En
| MEDLINE
| ID: mdl-1486276
Protein 4.1 is a multifunctional structural protein occupying a strategic position in the erythrocyte membrane. It is present in the erythrocyte membrane skeleton and in many nonerythroid cells. This report describes a novel method for purifying this protein based on its selective interaction with inositol hexaphosphate dimagnesium tetrapotassium salt. This interaction was discovered in the course of chromatography of high-salt extract of inside-out membrane vesicles on Procion orange MX-2R-Sepharose. The new procedure is simple and selective and produces protein 4.1 with better yield than that obtained with a previously published procedure. The purified protein 4.1 has the same immunoreactivity and the same alpha-chymotryptic digest profile as protein 4.1 purified by published methods and is fully functional in enhancing the interaction between F-actin and spectrin dimers.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ácido Fítico
/
Neuropéptidos
/
Cromatografía de Afinidad
/
Proteínas del Citoesqueleto
/
Membrana Eritrocítica
/
Proteínas de la Membrana
Límite:
Humans
Idioma:
En
Revista:
Protein Expr Purif
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
1992
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos