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. 1980 Jul 1;189(1):35–44. doi: 10.1042/bj1890035

A procedure for membrane-protein reconstitution and the functional reconstitution of the anion transport system of the human-erythrocyte membrane.

J M Wolosin
PMCID: PMC1161915  PMID: 7458905

Abstract

A short procedure for the isolation of band-3 protein, the protein responsible for anion exchange in erythrocytes, in a reasonable degree of purity was developed. Using this protein preparation and a novel procedure for membrane-protein reconstitution, vesicles displaying the basic features of the anion-exchange system of the erythrocyte were obtained. The reconstitution procedure is based on slow direct removal of Triton X-100 from aqueous lipid/detergent solutions. According to the composition of the reconstitution medium, either small single-walled or large multi-walled vesicles are obtained. The procedure conserves protein properties well, as is revealed by the similarity of the rates of SO4(2-) exchange in erythrocytes and reconstituted vesicles when corrected for the relevant volumes. A number of functional features of the exchange system were studied and compared with those of the native membrane.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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