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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2003-9-25
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pubmed:abstractText |
In the mixture of lipids and proteins which comprise pulmonary surfactant, the dominant protein by mass is surfactant protein A (SP-A), a hydrophilic glycoprotein. SP-A forms octadecamers that interact with phospholipid bilayer surfaces in the presence of calcium. Deuterium NMR was used to characterize the perturbation by SP-A, in the presence of 5 mM Ca(2+), of dipalmitoyl phosphatidylcholine (DPPC) properties in DPPC/egg-PG (7:3) bilayers. Effects of SP-A were uniformly distributed over the observed DPPC population. SP-A reduced DPPC chain orientational order significantly in the gel phase but only slightly in the liquid-crystalline phase. Quadrupole echo decay times for DPPC chain deuterons were sensitive to SP-A in the liquid-crystalline mixture but not in the gel phase. SP-A reduced quadrupole splittings of DPPC choline beta-deuterons but had little effect on choline alpha-deuteron splittings. The observed effects of SP-A on DPPC/egg-PG bilayer properties differ from those of the hydrophobic surfactant proteins SP-B and SP-C. This is consistent with the expectation that SP-A interacts primarily at bilayer surfaces.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14507703-11023905,
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
85
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2397-405
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14507703-1,2-Dipalmitoylphosphatidylcholine,
pubmed-meshheading:14507703-Binding Sites,
pubmed-meshheading:14507703-Eggs,
pubmed-meshheading:14507703-Lipid Bilayers,
pubmed-meshheading:14507703-Macromolecular Substances,
pubmed-meshheading:14507703-Magnetic Resonance Spectroscopy,
pubmed-meshheading:14507703-Membrane Fluidity,
pubmed-meshheading:14507703-Membranes, Artificial,
pubmed-meshheading:14507703-Molecular Conformation,
pubmed-meshheading:14507703-Phosphatidylglycerols,
pubmed-meshheading:14507703-Protein Binding,
pubmed-meshheading:14507703-Pulmonary Surfactant-Associated Protein A,
pubmed-meshheading:14507703-Temperature
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pubmed:year |
2003
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pubmed:articleTitle |
Interaction of pulmonary surfactant protein SP-A with DPPC/egg-PG bilayers.
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pubmed:affiliation |
Department of Physics and Physical Oceanography, Memorial University of Newfoundland, St. John's, Newfoundland, A1B 3X9 Canada. myke@physics.mun.ca
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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