CHARACTERIZATION OF HUMAN PULMONARY SURFACTANT PROTEINS ISOLATED FROM LUNG LAVAGE OF PATIENTS WITH PULMONARY ALVEOLAR PROTEINOSIS
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概要
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The isolation of human surfactant proteins from lung lavege of patients with pulmonary alveolar proteinosis and their influences on physiologucal properties of dipalmitoyl phosphatidylcholine (DPPC) were investigated. Pulmonary surfactant, obtained by discontinuous sucrose density gradient ultracentrifugation, was delipidated with ethanol-either, homogenized and incubated with Tris-saline buffer, pH 7.4, containing 0.1% sodium dodecyl sulfate at 37℃ for 1 h. After centrifugation, the supernatant protein solution which contained three proteins with apparent molecular weights of 32,000, 30,000 and 22,000 was subjected to gel filtration on Sephacryl S-200. Protein with molecular weight of 32,000 could not be separated because it had a tendency to aggregate. The other two separated proteins werre free of significant contaminations as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Adsorption rate of DPPC with or without additives of dipalmitoyl phosphatidylglycerol (DPPG) and two proteins was measured at 27℃. DPPC itself adsorbed to the air/liquid interface at very slow rate (half adsorption time; 118±4 min, mean±S.E.), but in the presence of 10% of DPPG, this mixture adsorbed rapidly (13±3 min). Furthermore, when each of the two preoteins was added to the mixture, the rate of adsorption was much more increased (1 to 4 min). These results suggest that the two active proteins isolated in this experiment are derived from some higher molecular weight proteins (the native surfactant proteins) and that they are involved in the formation of a micelle-like complex to change the physiological properties of surfactant phospholipids resulting in increased rate of adsorption.
- 名古屋市立大学の論文
- 1982-12-25