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• W2077087860 startingPage "320" @default.
• W2077087860 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." @default.
• W2077087860 created "2016-06-24" @default.
• W2077087860 creator A5001784443 @default.
• W2077087860 creator A5023957817 @default.
• W2077087860 date "1982-12-01" @default.
• W2077087860 modified "2023-09-26" @default.
• W2077087860 title "Myelin basic protein-enhanced fusion of membranes" @default.
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• W2077087860 doi "https://doi.org/10.1016/0005-2736(82)90438-2" @default.
• W2077087860 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6186278" @default.
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