Glycolipids are not extracted from phospholipid bilayers by binding to ferritin-lectin conjugates

Rhoderick E. Brown, Margaretta Allietta, Thomas W. Tillack, Thomas E. Thompson

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)495-499
Number of pages5
JournalBBA - Biomembranes
Volume731
Issue number3
DOIs
StatePublished - Jun 23 1983
Externally publishedYes

Keywords

  • Electron microscopy
  • Ferritin-ricin conjugate
  • Freeze-etching
  • Glycosphingolipid anchoring
  • Phosphatidylcholine bilayer

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