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Glycophorin, extracted from the erythrocyte membrane after treatment with lithium-diiodo-salicylate, still contains a significant amount of phospholipid, consisting predominantly of phosphatidylserine. Methods are described which lead to a full delipidation of the protein. After treatment with neuraminidase, delipidated glycophorin shows a preferential interaction with monolayers of negatively-charged phospholipids. This lipid-protein interaction is decreased by the presence of cholesterol in the lipid film.
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