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  • Title: Annexins IV (p32) and VI (p68) interact with erythrocyte membrane in a calcium-dependent manner.
    Author: Bandorowicz J, Pikuła S, Sobota A.
    Journal: Biochim Biophys Acta; 1992 Apr 13; 1105(2):201-6. PubMed ID: 1534024.
    Abstract:
    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.
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