Annexins IV (p32) and VI (p68) interact with erythrocyte membrane in a calcium-dependent manner.
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 microM Ca2+. The maximal binding was estimated as 2 micrograms of annexin VI per 1 microgram or erythrocyte membrane protein, in the presence of 100 microM Ca2+. The property of erythrocyte membrane to interact with annexins was utilized in preparation of a affinity-column with polyacrylamide-immobilized erythrocyte membrane.
Bandorowicz
J
J
Department of Cell Biology, Nencki Institute of Experimental Biology, Warsaw, Poland.
Pikuła
S
S
Sobota
A
A
D000818:Animals; D017317:Annexin A6; D017302:Annexins; D002118:Calcium / Q000378:metabolism*; D002135:Calcium-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D008099:Liver / Q000737:chemistry; D009000:Monocytes / Q000737:chemistry; D011257:Pregnancy Proteins / Q000302:isolation & purification / Q000378:metabolism*; D013552:Swine
D017317:Annexin A6; D017302:Annexins; D002135:Calcium-Binding Proteins; D011257:Pregnancy Proteins; D002118:Calcium