Study of the apoprotein of Folch-Pi bovine proteolipid. II. Characterization of the components isolated from sodium dodecyl sulfate solutions.

Acrylamide gel electrophoresis in dodecyl sulfate solutions of Folch-Pi apoprotein shows several bands. The different components were separated by Biogel P-200 filtration and then reduced and carboxymethylated. A comparative study of the amino acid composition, N-terminal sequence and C-terminal amino acid of the different components led to the assumption that their primary sequences are similar.