[Rate of interaction of ferricytochrome c with negatively charged liposomes from natural lecithin: effect of the physicochemical state of the membrane hydrophobic layer].
Viktor V. Obraztsov, А. А. Селищева, В.С. Данилов
Abstract
Viktor V. Obraztsov, А. А. Селищева, В.С. Данилов
Abstract
The absorption velocity of ferricytochrome c on the surface of liposomes from egg lecithin containing 10% of lauric acid was studied. Liposomes were prepared from lecithin of three fractions which differed by the composition of fatty acids, unsaturation and the lipid interaction decreased at the temperature below T phi pi for lecithin fractions containing larger quantity of saturated fatty acids. An opposite tendency was observed for the temperature above T phi pi. In the phase transition region of lecithin of refractory fraction the local maximum of protein-lipid interaction was observed. Judging by the character of the changes of the values of energy activation, small additions of cholesterol in the membrane loosen the bilayer at the temperature below T phi pi and condense it at above T phi pi. The data obtained are discussed in terms of the effect of the state of molecule hydrophobic part on the velocity of protein-lipid interaction.
A significance statement is not available in the OpenAlex record.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
The absorption velocity of ferricytochrome c on the surface of liposomes from egg lecithin containing 10% of lauric acid was studied. Liposomes were prepared from lecithin of three fractions which differed by the composition of fatty acids, unsaturation and the lipid interaction decreased at the temperature below T phi pi for lecithin fractions containing larger quantity of saturated fatty acids. An opposite tendency was observed for the temperature above T phi pi. In the phase transition region of lecithin of refractory fraction the local maximum of protein-lipid interaction was observed. Judging by the character of the changes of the values of energy activation, small additions of cholesterol in the membrane loosen the bilayer at the temperature below T phi pi and condense it at above T phi pi. The data obtained are discussed in terms of the effect of the state of molecule hydrophobic part on the velocity of protein-lipid interaction.
Key concepts: Lecithin, Egg lecithin, Liposome, Degree of unsaturation, Chemistry, Bilayer, Chromatography, Membrane