Myelin basic protein-enhanced fusion of membranes

Paul D. Lampe, Gary L. Nelsestuen

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

Myelin basic protein caused rapid aggregation of vesicles containing acidic phospholipids. Aggregation could be reversed by trypsin digestion of the myelin basic protein. Aggregated vesicles containing gel phase phospholipids or vesicles containing greater than 15 mol% lysolecithin underwent fusion. The extent of fusion was measured by irreversible changes in the light-scattering intensities or diffusion coefficients of the vesicles. Fusion was also measured by the fluorescence quenching which occurred when vesicles containing a covalently bound fluorophore, N-4-nitrobenzo-2-oxa-1,3-diazole, were fused with vesicles containing the covalently bound spin label, 4,4-dimethyl-oxazolidine-N-oxyl. The kinetics of fusion were first order in phospholipid and had half-times of 0.5-5 min depending on lysolecithin composition. This protein-enhanced membrane fusion may provide a valuable model system for studying some types of biological membrane fusions.

Original languageEnglish (US)
Pages (from-to)320-325
Number of pages6
JournalBBA - Biomembranes
Volume693
Issue number2
DOIs
StatePublished - Dec 22 1982

Keywords

  • Fluorescence
  • Light scattering
  • Membrane fusion
  • Myelin basic protein

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