[Common and peculiar features of the interaction of hemoglobins with hydrated dipalmitoyllecithin].

It was demonstrated that human and horse hemoglobin variants having quantitative difference in the interaction with dipalmitoyllecithin exhibit features of generality. The latter is manifested in the established hydrophobic contacts between protein and lipid in hydrated films discovered by IR spectroscopy. The arrangement of hydrophobicity profiles of hemoproteins demonstrated in amino acid sequences of chains the existence of intermittent hydrophobic and hydrophilic regions. Such a composition of hemoglobins could underlie their property to participate in hydrophobic interactions with lipids.