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• W1612222625 abstract "Abstract of the dissertation entitled INTERACTIONS OF LUNG SURFACTANT LIPIDS WITH PROTEINS OF THE ALVEOLAR SPACE submitted by Peter Pagast in partial fulfillment of the requirements for the degree of Doctor of Philosophy, June, 1975.of the dissertation entitled INTERACTIONS OF LUNG SURFACTANT LIPIDS WITH PROTEINS OF THE ALVEOLAR SPACE submitted by Peter Pagast in partial fulfillment of the requirements for the degree of Doctor of Philosophy, June, 1975. Dipalmitoyl phosphatidyl choline (DPC) is the major component of extracellular pulmonary surfactant. Model studies show it to be the primary constituent of surfactant responsible for the lowering of the surface tension in the alveolar air liquid interphase, which is essential for the respiratory process. There is little information as to the biochemical or physiological function of other lipids and the proteins found in the pulmonary surfactant. However, on isolation of pulmonary surfactant by the procedure of Frosolono .!!.! !:!.• (J. Lipid Res. .!!., 439-457, 1970), it is shown to consist of lipid-protein complexes with a consistent phospholipid to protein ratio. This work studies the composition, the physical, and the spectral properties of native and artificial model phospholipid-protein complexes for pulmonary surfactant. Dog alveolar surfa~tant was isolated and separated into its constituent lipid and protein components by partition chromatography over Sephadex LH-20 in 2-chloroethanol-water. A series of experiments resulting in reconstitution of surfactant lipidprotein complexes were performed to investigate the interaction of surfactant lipids with surfactant proteins. Reconstitution of the lipid and protein of the surfactant fraction of dog resulted in the formation of lipid-protein complexes which compared favorably with the original isolated surfactant complexes. These complexes were characterized by certain well-defined properties including their density, particle size, phospholipid to protein ratio, protein composition and circular dichroism. Reconstitution experiments were performed substituting delipidated albumin and delipidated dog serum proteins in place of surfactant proteins. Also, reconstitution experiments were performed utilizing commercial phosphatidylcholine in place of surfactant lipids• In all these experiments only a small yield of lipid-protein complexes were found, and the complex that did form had different physical and spectral properties from the reconstituted complex utilizing pulmonary surfactant lipids and proteins. When pulmonary extracellular proteins other than found in the pulmonary surfactant fraction were utilized in place of surfactant proteins in reconstitution experiments,_ the yield of phospholipid-protein complexes was high. However, the density of the complexes were di££use and dissimilar from that of native complexes. The a-helix content of the reconstituted complexes in SDS was higher than that of the delipidated apoprotein. A similar increase in a-helix content was not observed following reconstitution of surfactant 1ipids with de1ipidated protein from surface inactive fractions of 1ung washing, serum, or bovine albumin. Likewise, reconstitution of commercia1 phosphatidy1choline with surfactant protein was not associated with increased a-he1ix content of the formed complex. In a discontinuous gradient, the reconstituted 1ipid-protein comp1exes of the surfactant fraction appeared as a single band on a sucrose gradient, whi1e complexes of surfactant 1ipids with de1ipidated dog serum proteins or extrace1lular proteins of the 1ung other than found in the pulmonary surfactant fraction displayed a wide range of distributions on a sucrose gradient. Negatively stained preparations examined by electron microscopy demonstrated that the original surfactant fractions (obtained by a procedure involving sedimentation) contained large aggregates of liposomes widely varying in size and more uniformly distributed. The liposomes of reconstituted complexes were similar in size and distribution to those found in lung washing. SDS-polyacrylamide gel electrophoresis showed that the pro, tein composition of surfactant fraction was similar to that of serum, but two additional bands with approximate molecular weights of 11,000 and J5,000 were only seen in proteins of the surfactant fraction, and comprised 15 per cent of the surfactant proteins. The distribution of the individual proteins comprising the surfactant protein fraction did not change on reconstitution. Analysis of the protein in originally isolated and reconstituted" @default.
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• W1612222625 date "1975-01-01" @default.
• W1612222625 modified "2023-09-26" @default.
• W1612222625 title "Interaction of Lung Surfactant Lipids with Proteins of the Alveolar Space" @default.
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