title: Interaction of myelin basic protein and proteolipid protein.
abstract: The interaction of myelin basic protein (MBP) and proteolipid protein (PLP) was studied using a microtitre well binding assay and the ligand-blot overlay technique. The binding of iodinated PLP to MBP that was immobilized on microtitre wells was saturable and reversible. Its selectivity was investigated by the ligand-blot overlay technique. Iodinated PLP was found to bind MBP but not any other CNS myelin proteins. This interaction was not dependent on the phosphoryl moiety of MBP. Binding of PLP to histone H4 also occurred, but the amount of PLP bound per unit MBP was greater than for this histone.
authors: Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
authors: A M
authors: AM
authors: Edwards
authors: N W
authors: NW
authors: Ross
authors: J B
authors: JB
authors: Ulmer
authors: P E
authors: PE
authors: Braun
mesh_terms: D000818:Animals; D001923:Brain Chemistry; D051379:Mice; D004676:Myelin Basic Protein / Q000378:metabolism*; D009185:Myelin Proteins / Q000378:metabolism*; D018991:Myelin Proteolipid Protein
chemical_list: D004676:Myelin Basic Protein; D009185:Myelin Proteins; D018991:Myelin Proteolipid Protein