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Journal Article

Band 3 protein—cholesterol interactions in erythrocyte membranes. Possible role in anion transport and dependency on membrane phospholipid

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Schubert,  Dieter
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Boss,  Karin
Department of Cell Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Schubert, D., & Boss, K. (1982). Band 3 protein—cholesterol interactions in erythrocyte membranes. Possible role in anion transport and dependency on membrane phospholipid. FEBS Letters, 150(1), 4-8. doi:10.1016/0014-5793(82)81295-7.


Cite as: https://hdl.handle.net/21.11116/0000-0008-1A5D-4
Abstract
Band 3 protein of the human erythrocyte membrane, the anion transport protein, possesses a high affinity steroid binding site. In mixed phospholipid—cholesterol monolayers, the state of occupancy of this site is positively correlated with their cholesterol and sphingomyelin content and negatively with their glycerophospholipid content. We suggest that, in the erythrocyte membrane, the binding site is an inhibitory site of anion transport and that the modulation of its state of occupancy by the membrane lipid is responsible for the negative correlation of anion transport with the membrane's content of cholesterol and sphingomyelin and the positive correlation with the phosphatidylcholine content