ANNEXINS-IV (P-32) AND ANNEXINS-VI (P68) INTERACT WITH ERYTHROCYTE-MEMBRANE IN A CALCIUM-DEPENDENT MANNER

被引：31

作者：

BANDOROWICZ, J

PIKULA, S

SOBOTA, A

机构：

[1] M NENCKI INST EXPTL BIOL,DEPT CELL BIOL,3 PASTEUR STR,PL-02093 WARSAW,POLAND

[2] M NENCKI INST EXPTL BIOL,DEPT MUSCLE BIOCHEM,PL-02093 WARSAW,POLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1105卷 / 02期

关键词：

ANNEXIN; ERYTHROCYTE PLASMA MEMBRANE; MEMBRANE-PROTEIN INTERACTION; (PORCINE LIVER);

D O I：

10.1016/0005-2736(92)90195-R

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Purification of annexin IV and VI from porcine liver was achieved by Mono Q ion exchange chromatography at pH 8.9 and pH 7.5, respectively. The isolated proteins interacted with erythrocyte membrane as function of calcium ion and the protein concentration. Half-maximal binding of annexin VI to erythrocyte membrane was found to occur at 8-mu-M Ca2+. The maximal binding was estimated as 2-mu-g of annexin VI per 1-mu-g or erythrocyte membrane protein, in the presence of 100-mu-M Ca2+. The property of erythrocyte membrane to interact with annexins was utilized in preparation of a affinity-column with polyacrylamide-immobilized erythrocyte membrane.

引用

页码：201 / 206

页数：6

共 34 条

[1] A ROLE FOR CALPACTIN IN CALCIUM-DEPENDENT EXOCYTOSIS IN ADRENAL CHROMAFFIN CELLS [J].