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- W2087630478 abstract "We have prepared cholesterol- and sphingolipid-rich membrane microdomains, termed lipid rafts, from human erythrocytes by Triton X-100 lysis in the cold, centrifugation of the detergent-insoluble complexes, and flotation of the low buoyant density material by sucrose gradient centrifugation. A glycosyl phosphatidylinositol (GPI)-anchored enzyme, acetylcholine esterase, was used as a lipid raft marker. The major protein components were identified as stomatin (erythrocyte band 7.2b), flotillin-1, and flotillin-2. These are cytoplasmically oriented, integral membrane proteins, which are distantly related (stomatin superfamily). A part of the major cytoskeletal proteins, spectrin, actin, band 4.1, and band 4.2, was also associated with the lipid rafts, but could be stripped from the rafts by an alkaline buffer. Stomatin and the flotillins are oligomeric proteins, which probably act as separate scaffolding components at the cytoplasmic face of erythrocyte lipid rafts. The isolated, cytoskeleton-free lipid rafts were immobilized by binding to wheat germ agglutinin-coated mica supports, in order to get adsorption via the extracellular glycoproteins and to expose the cytosolic side of the rafts. Atomic Force Microscopy revealed large membrane patches of several hundred nm in size, but also round, vesicle-like structures of about 300 nm diameter (Figure 1)." @default.
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- W2087630478 date "2001-07-01" @default.
- W2087630478 modified "2023-09-26" @default.
- W2087630478 title "Isolation, Biochemical Characterization, and Atomic Force Microscopy of Erythrocyte Lipid Rafts" @default.
- W2087630478 doi "https://doi.org/10.1002/1438-5171(200107)2:2<135::aid-simo135>3.0.co;2-p" @default.
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