As birds have tubular lungs that do not contain alveoli, avian surfactant p
redominantly functions to maintain airflow in tubes rather than to prevent
alveolar collapse. Consequently, we have evaluated structural, biochemical,
and functional parameters of avian surfactant as a model for airway surfac
tant in the mammalian lung. Surfactant was isolated from duck, chicken, and
pig lung lavage fluid by differential centrifugation. Electron microscopy
revealed a uniform surfactant layer within the air capillaries of the bird
lungs, and there was no tubular myelin in purified avian surfactants. Phosp
hatidylcholine molecular species of the various surfactants were measured b
y HPLC. Compared with pig surfactant, both bird surfactants were enriched i
n dipalmitoylphosphatidylcholine, the principle surface tension-lowering ag
ent in surfactant, and depleted in palmitoylmyristoylphosphatidylcholine, t
he other disaturated phosphatidylcholine of mammalian surfactant. Surfactan
t protein (SP)-A was determined by immunoblot analysis, and SP-B and SP-C w
ere determined by gel-filtration HPLC. Neither SP-A nor SP-C was detectable
in either bird surfactant, but both preparations of surfactant contained S
P-B. Surface tension function was determined using both the pulsating bubbl
e surfactometer (PBS) and capillary surfactometer (CS). Under dynamic cycli
ng conditions, where pig surfactant readily reached minimal surface tension
values below 5 mN/m, neither avian surfactant reached values below 15 mN/m
within 10 pulsations. However, maximal surface tension of avian surfactant
was lower than that of porcine surfactant, and all surfactants were equall
y efficient in the CS. We conclude that a surfactant composed primarily of
dipalmitoylphosphatidylcholine and SP-B is adequate to maintain patency of
the air capillaries of the bird lung.