Protein was isolated from bovine lung and extracted with organic solvents of varying polarities. Lipid represented 20% by weight of the total isolate, and the amount extracted depended on the polarity of the organic solvents employed. Phospholipids, cholesterol and free fatty acids were the lipid classes detected, phospholipids being the major component left after solvent extraction. Water absorption characteristics, solubility of the protein and superficial hydrophobicity were related to the amount of lipids left after solvent extraction. The results indicated that the lipids rather than the organic solvents used for lipid removal affected protein characteristics. Phospholipid-protein interactions seem to induce, on the protein, greater amounts of ordered conformation.