Phospholipid vesicle aggregation induced by human myelin basic protein.
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.
D001120:Arginine / Q000031:analogs & derivatives / Q000032:analysis; D002499:Centrifugation, Density Gradient; D006801:Humans; D008051:Lipid Bilayers / Q000378:metabolism*; D008081:Liposomes; D009103:Multiple Sclerosis / Q000503:physiopathology*; D004676:Myelin Basic Protein / Q000502:physiology*; D010713:Phosphatidylcholines / Q000378:metabolism*; D011485:Protein Binding; D013329:Structure-Activity Relationship
D008051:Lipid Bilayers; D008081:Liposomes; D004676:Myelin Basic Protein; D010713:Phosphatidylcholines; C024917:symmetric dimethylarginine; D001120:Arginine