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- W2024583017 abstract "Lipid—protein monolayers of various lipids mixed with either β-lactoglobulin, bovine serum albumin, or β-casein were transferred from the air-water interface to mica substrates and examined by electron microscopy. Phospholipids and triglycerides which gave condensed films at the air—water interface did not mix with proteins in monolayers as shown by electron micrographs of the transferred films. Heterogeneous films were observed with as little as 5 mole (residue) percent phosphatidic acid or tristearin in the mixed films, suggesting little, if any, solubility of condensed lipids in protein before the onset of phase separation. Homogeneous lipid—protein films were observed when the mixed monolayers were prepared from phospholipids or triglycerides that exhibit expanded behavior at the air—water interface. Fatty acids did not always follow this behavior pattern. Stearic acid, which forms a condensed film at the air—water interface, did not separate from the protein in a mixed film until the lipid content exceeded 10–15 mole (residue) percent. Nervonic acid, which exhibits condensed behavior at high pressure and room temperature, also did not separate from protein in mixed films under these conditions. Film balance experiments suggest that lipid—protein interactions may be hindering segregation of nervonic acid from proteins in monolayers." @default.
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- W2024583017 title "Miscibility in lipid—protein monolayers" @default.
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