Isolation and purification of myelin proteolipid protein using high speed gel filtration in sodium dodecyl sulfate.

Small and preparative gel filtration columns were studied for high pressure liquid chromatography of myelin proteins in sodium dodecyl sulfate. The preparative column proved useful for isolating and purifying proteolipid protein almost free (0.3-0.5%) of myelin basic protein as demonstrated by SDS-PAGE, MBP RIA, and immunoblotting. The small columns were not as useful as SDS-PAGE for analytical purposes.