| Literature DB >> 1534024 |
J Bandorowicz1, S Pikuła, A Sobota.
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.Entities:
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Year: 1992 PMID： 1534024 DOI： 10.1016/0005-2736(92)90195-r
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002