title: The role of charge microheterogeneity of human myelin basic protein in the formation of phosphatidylglycerol multilayers.
abstract: Human myelin basic protein (HBP) was fractionated into its various charge isomers by chromatography on CM-52 columns at pH 10.6. Components 1,2,3 and "8" (C-1, C-2, C-3, and C-"8") were cleanly separated. Each component was combined with phosphatidylglycerol (PG) vesicles, at neutral pH at a concentration of 30% (w/w), protein/lipid. C-1, the most cationic of the components was the most effective at inducing the formation of multilayers when studied by liquid X-ray diffraction. C-3, which differs from C-1 by 2 positive charges was less effective than C-2. C-"8" was totally ineffective since the scattering pattern with this component was no different from that of the pure lipid. Thus a seemingly small change in net charge of the protein had a dramatic effect on the ability of the protein to organize the lipid into a crystalline, multilayer arrangement characteristic of compact myelin.
authors.forename: G W
authors.initials: GW
authors.lastname: Brady
authors.forename: D B
authors.initials: DB
authors.lastname: Fein
authors.forename: D D
authors.initials: DD
authors.lastname: Wood
authors.forename: M A
authors.initials: MA
authors.lastname: Moscarello
mesh_terms: D002845:Chromatography / Q000379:methods; D004563:Electrochemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007536:Isomerism; D008563:Membrane Lipids / Q000378:metabolism*; D004676:Myelin Basic Protein / Q000378:metabolism*; D010715:Phosphatidylglycerols / Q000378:metabolism*; D014961:X-Ray Diffraction
chemical_list: D008563:Membrane Lipids; D004676:Myelin Basic Protein; D010715:Phosphatidylglycerols