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.