| pubmed-article:14507703 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14507703 | lifeskim:mentions | umls-concept:C0034085 | lld:lifeskim |
| pubmed-article:14507703 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:14507703 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:14507703 | lifeskim:mentions | umls-concept:C1420002 | lld:lifeskim |
| pubmed-article:14507703 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:14507703 | pubmed:dateCreated | 2003-9-25 | lld:pubmed |
| pubmed-article:14507703 | 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. | lld:pubmed |
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| pubmed-article:14507703 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14507703 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14507703 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14507703 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14507703 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14507703 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:14507703 | pubmed:author | pubmed-author:MorrowMichael... | lld:pubmed |
| pubmed-article:14507703 | pubmed:author | pubmed-author:KeoughKevin... | lld:pubmed |
| pubmed-article:14507703 | pubmed:author | pubmed-author:StewartJuneJ | lld:pubmed |
| pubmed-article:14507703 | pubmed:author | pubmed-author:Abu-LibdehNid... | lld:pubmed |
| pubmed-article:14507703 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14507703 | pubmed:volume | 85 | lld:pubmed |
| pubmed-article:14507703 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14507703 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14507703 | pubmed:pagination | 2397-405 | lld:pubmed |
| pubmed-article:14507703 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:14507703 | pubmed:meshHeading | pubmed-meshheading:14507703... | lld:pubmed |
| pubmed-article:14507703 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14507703 | pubmed:articleTitle | Interaction of pulmonary surfactant protein SP-A with DPPC/egg-PG bilayers. | lld:pubmed |
| pubmed-article:14507703 | pubmed:affiliation | Department of Physics and Physical Oceanography, Memorial University of Newfoundland, St. John's, Newfoundland, A1B 3X9 Canada. myke@physics.mun.ca | lld:pubmed |
| pubmed-article:14507703 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14507703 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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