PURIFICATION OF ERYTHROCYTE PROTEIN-4.1 BY SELECTIVE INTERACTION WITH INOSITOL HEXAPHOSPHATE

被引：10

作者：

ELOUGGOUTI, S ^{[1
]}

BOURNIER, O ^{[1
]}

BOIVIN, P ^{[1
]}

BERTRAND, O ^{[1
]}

DHERMY, D ^{[1
]}

机构：

[1] CTS,INSERM,U76,F-75739 PARIS 15,FRANCE

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1992年 / 3卷 / 06期

关键词：

D O I：

10.1016/1046-5928(92)90066-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 α-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. © 1992.

引用

页码：488 / 496

页数：9

共 53 条

[1]

ANDERSON RA, 1989, RED BLOOD CELL MEMBR, P187

[2]

BATTEN A, 1989, P AM ASSOC CANC RES, V30, P182

[3] A MALACHITE GREEN PROCEDURE FOR ORTHO-PHOSPHATE DETERMINATION AND ITS USE IN ALKALINE PHOSPHATASE-BASED ENZYME-IMMUNOASSAY [J].