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Abstract

The extracellular lung surfactant surface film (ELSSF) which lines the mammalian lung alveoli at the alveolar air-aqueous cell surface interface is vital in both the breathing and the pulmonary defence processes. The molecular composition of, the structure of and the interaction in the ELSSF was studied, after the ELSSF of human lung lavages could be separated from the subphase and reassembled from its components by using the multicompartment Fromherz-type Langmuir-Blodgett trough. Transmission electron microscopy images of immunogold- labelled and negatively stained isolated film specimens were seen in a continuous layer of mostly phospholipid head groups surfactant-specific protein SpA molecules. Electrical double-layer capacitance and oxygen reduction potential measurements carried out by transferring the surface film from the air-water to a mercury-saline interface of a hanging mercury drop electrode revealed a strong lipid-protein SpA interaction. SpA molecules were partly squeezed out from the film by compression; a proteinless lipid film proved to be a condensed multilayer. Contact with SpA transformed the multilayer into a loose monomolecular film. It is suggested that SpA molecules play a lipid-transporting role, removing lipids in excess from the air-water interface into the aqueous subphase and vice versa. Lipid- protein interaction can be of importance in vivo. An explanation of how the surfactant film works during the two phases of breathing is proposed.