Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates |
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Authors: | Rhoderick E Brown Margaretta Allietta Thomas W Tillack Thomas E Thompson |
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Institution: | 1. Department of Biochemistry, University of Virginia School of Medicine, Charlottesville, VA 22908 U.S.A.;2. Department of Pathology, University of Virginia School of Medicine, Charlottesville, VA 22908 U.S.A. |
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Abstract: | A radioactively-labelled glycosphingolipid, asialo-GM1, has been incorporated into phosphatidylcholine multilamellar vesicles. After incubation with ferritin-Ricinus communis agglutinin 60 (RCA 60) conjugate at different temperatures, the vesicles were separated from the conjugate by discontinuous density gradient ultracentrifugation. Measurement of the distribution of the radioactively-labelled asialo-GM1 in the pelleted conjugate fraction and freeze-etch electron microscopy of the vesicle fraction indicate that the decrease in labelling of vesicles by ferritin-RCA 60 conjugate with increasing temperatures (Tillack, T.W., Wong, M., Allietta, M. and Thompson, T.E. (1982) Biochim. Biophys. Acta 691, 261–273) reflects a decrease in apparent binding affinity rather than an ability of the conjugate to extract glycolipid from the phospholipid bilayer after binding. |
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Keywords: | Glycosphingolipid anchoring Phosphatidylcholine bilayer Ferritin-ricin conjugate Freeze-etching Electron microscopy DMPC dimyristoylphosphatidylcholine POPC palmitoyloleoylphosphatidylcholine RCA 60 |
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