Purification of erythrocyte protein 4.1 by selective interaction with inositol hexaphosphate. |
| |
Authors: | S el Ouggouti O Bournier P Boivin O Bertrand D Dhermy |
| |
Affiliation: | INSERM U 160, H?pital Beaujon, Clichy, France. |
| |
Abstract: | 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. |
| |
Keywords: | |
|
|