Lipid-protein interactions with native and modified myelin basic protein.
The basic protein of central nervous system myelin has been shown to form complexes with acidic lipids in vitro. We measured the interaction of myelin basic protein with several charged and neutral lipids in a biphasic chloroform/methanol/water system and investigated the effect of decreasing the electrical charge of the basic amino groups of the myelin basic protein by acetylation. The modified myelin basic protein, which has an average of eight acetyl residues incorporated, was characterised by gel electrophoresis and circular dichroism. Complexes formed between the acetylated myelin basic protein and acidic lipids exhibited a reduction in the amount of lipids bound, a value that could be correlated with the number of modified amino groups. The significance of these experiments with reference to protein-lipid interaction in the myelin membrane is discussed.
D000818:Animals; D001921:Brain; D002417:Cattle; D002554:Cerebrosides; D002784:Cholesterol; D002942:Circular Dichroism; D007700:Kinetics; D008055:Lipids; D009185:Myelin Proteins; D010712:Phosphatidic Acids; D010713:Phosphatidylcholines; D010716:Phosphatidylinositols; D011485:Protein Binding; D011487:Protein Conformation; D013433:Sulfoglycosphingolipids
D002554:Cerebrosides; D008055:Lipids; D009185:Myelin Proteins; D010712:Phosphatidic Acids; D010713:Phosphatidylcholines; D010716:Phosphatidylinositols; D013433:Sulfoglycosphingolipids; D002784:Cholesterol