HYDROPHOBIC PROTEINS OF LAMELLATED OSMIOPHILIC BODIES ISOLATED FROM PIG LUNG

In addition to proteins that are insoluble in organic solvents, lamellated bodies isolated from pig lung and surfactant prepared from bronchopulmonary lavage fluid contain another group of proteins that are extracted together with lipid into the large organic phase. These hydrophobic proteins constitute about 40% of the total protein of lamellated bodies and about 13% of the total protein of surfactant isolated from lavage fluid, whereas less than 1% of the total protein of pig lung microsomal fraction and mitochondria is extracted by organic solvents. The hydrophobic proteins of lamellated bodies were separated into four fractions and freed from phospholipid by chromatographic procedures. Their apparent molecular weights vary between 11500 and 16500, they contain 62-79% of hydrophobic residues and 16-22% of sulphur-containing amino-acids, and leucine is the major N-terminal amino acid in each case.