Brain proteolipids. Isolation, purification and effect on ionic permeability of membranes.
Proteolipid apoproteins have been isolated from a whole bovine brain homogenate by chloroform/methanol extraction, and fractionated by chromatography on modified (lipophilic) Sephadex, followed by ion-exchange chromatography on CM-Trisacryl. The various final, highly hydrophobic, fractions are homogeneous (sodium dodecyl sulfate/polyacrylamide gel electrophoresis). Transmembrane ion transfers were studied by 22Na + flux and electrical conductance measurements. Single channel events were observed at low protein concentrations, in particular with one of the final homogeneous apoproteolipids of molecular mass 24 kDa.
D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002463:Cell Membrane Permeability; D055598:Chemical Phenomena; D002621:Chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D008563:Membrane Lipids / Q000302:isolation & purification* / Q000502:physiology; D011510:Proteolipids / Q000302:isolation & purification* / Q000502:physiology
D000596:Amino Acids; D008563:Membrane Lipids; D011510:Proteolipids