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Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates
Authors:Rhoderick E Brown  Margaretta Allietta  Thomas W Tillack  Thomas E Thompson
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.
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 asialo-GM1-containing 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.
Keywords:Glycosphingolipid anchoring  Phosphatidylcholine bilayer  Ferritin-ricin conjugate  Freeze-etching  Electron microscopy  DMPC  dimyristoylphosphatidylcholine  POPC  palmitoyloleoylphosphatidylcholine  RCA 60
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