Phospholipid vesicle aggregation induced by human myelin basic protein
- 1 February 1984
- journal article
- research article
- Published by Springer Nature in Neurochemical Research
- Vol. 9 (2) , 241-248
- https://doi.org/10.1007/bf00964172
Abstract
Human myelin basic protein isolated from the brains of individuals who died with multiple sclerosis was more potent in inducing the aggregation of egg phosphatidylcholine vesicles than was the basic protein isolated from the brains of normal individuals. The portion of myelin basic protein which bound to egg phosphatidylcholine vesicles was separated from the free protein by sucrose density gradient centrifugation. Similar amounts of basic protein from normal or from multiple sclerosis brains are bound to the lipid and no consistent differences in the NG, N′G dimethyl-arginine content of the protein fractions have been found.Keywords
This publication has 22 references indexed in Scilit:
- Stopped-flow studies of myelin basic protein association with phospholipid vesicles and subsequent vesicle aggregationBiochemistry, 1983
- Myelin basic protein-enhanced fusion of membranesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1982
- The effect of bovine myelin basic protein on the phase transition properties of sphingomyelinBiochimica et Biophysica Acta (BBA) - Biomembranes, 1982
- The interaction of basic proteins from normal and multiple sclerosis myelin with phosphatidylglycerol vesiclesFEBS Letters, 1981
- Structural organization of the human myelin membraneBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1978
- Conformational studies on carbon-13-enriched human and bovine myelin basic protein, in solution and incorporated into liposomesBiochemistry, 1978
- Effect of basic protein from human central nervous system myelin on lipid bilayer structureThe Journal of Membrane Biology, 1978
- Non-covalent cross-linking of lipid bilayers by myelin basic protein. A possible role in myelin formationBiochimica et Biophysica Acta (BBA) - Biomembranes, 1977
- Specific interaction of central nervous system myelin basic protein with lipids. Specific regions of the protein sequence protected from the proteolytic action of trypsinBiochimica et Biophysica Acta (BBA) - Biomembranes, 1973
- X-ray diffraction and electron microscope study of the interactions of myelin components. The structure of a lamellar phase with a 150 to 180 Å repeat distance containing basic proteins and acidic lipidsJournal of Molecular Biology, 1973