rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1994-8-24
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pubmed:abstractText |
Spread binary monolayers of surfactant-associated proteins SP-B and SP-C were formed at the air-water interface. Surface pressure measurements showed no interactions between the hydrophobic proteins. The effects of a mixture of SP-B plus SP-C (2:1, w/w) on the properties of monolayers of dipalmitoylphosphatidylcholine (DPPC), dipalmitoylphosphatidylglycerol (DPPG), and DPPC:DPPG (7:3, mol:mol) were studied. During compression of ternary and quaternary films, containing less than 0.4 mol% or 5 weight% total protein, the proteins were not squeezed out and appeared to remain associated with the film until collapse at surface pressures of about 65-70 mN.m-1. At initial concentrations of total protein of about 0.9 mol% or 10 weight%, exclusion of protein-lipid complexes was observed at 40-50 mN.m-1. Larger amounts of phospholipid were removed by proteins from (SP-B:SP-C)/DPPG films than from (SP-B:SP-C)/DPPC ones. Separate squeeze-out of SP-B (or SP-B plus DPPC) at about 40 mN.m-1, followed by exclusion of SP-C (or SP-C plus DPPC) at about 50 mN.m-1, was observed in (SP-B:SP-C)/DPPC films. This led to a conclusion that there was independent behavior of SP-B and SP-C in (SP-B:SP-C)/DPPC monolayers. The quaternary (SP-B:SP-C)/(DPPC:DPPG) films showed qualitatively similar process of squeeze-out of the proteins. In the ternary mixtures of SP-B plus SP-C with DPPG separate exclusion of SP-B was not detected; rather, the data was consistent with exclusion of a (SP-B:SP-C)/DPPG complex at about 50 mN.m-1. The results imply possible interactions between SP-B and SP-C and the acidic phospholipid.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1,2-Dipalmitoylphosphatidylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/1,2-dipalmitoylphosphatidylglycerol,
http://linkedlifedata.com/resource/pubmed/chemical/Membranes, Artificial,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylglycerols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Proteolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Pulmonary Surfactants,
http://linkedlifedata.com/resource/pubmed/chemical/Water
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
|
pubmed:issn |
0006-3495
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
66
|
pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1158-66
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8038387-1,2-Dipalmitoylphosphatidylcholine,
pubmed-meshheading:8038387-Air,
pubmed-meshheading:8038387-Animals,
pubmed-meshheading:8038387-Biophysical Phenomena,
pubmed-meshheading:8038387-Biophysics,
pubmed-meshheading:8038387-Membranes, Artificial,
pubmed-meshheading:8038387-Phosphatidylglycerols,
pubmed-meshheading:8038387-Phospholipids,
pubmed-meshheading:8038387-Pressure,
pubmed-meshheading:8038387-Proteolipids,
pubmed-meshheading:8038387-Pulmonary Alveoli,
pubmed-meshheading:8038387-Pulmonary Surfactants,
pubmed-meshheading:8038387-Surface Properties,
pubmed-meshheading:8038387-Swine,
pubmed-meshheading:8038387-Water
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pubmed:year |
1994
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pubmed:articleTitle |
Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: III. Proteins SP-B plus SP-C with phospholipids in spread monolayers.
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pubmed:affiliation |
Department of Biochemistry, Memorial University of Newfoundland, St. John's, Canada.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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