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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
1999-2-23
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pubmed:abstractText |
Pulmonary surfactant-specific protein, SP-C, isolated from porcine lung lavage, has been deacylated to investigate the role of the two thioester linked palmitoyl chains located near the N-terminus. Surface thermodynamic properties, secondary structure, and orientation of native and deacylated SP-C in 1, 2-dipalmitoylphosphatidylcholine (DPPC) monolayers has been characterized by combined surface pressure-molecular area (pi-A) isotherms and infrared reflection-absorption spectroscopy (IRRAS) measurements. The isotherms indicate that deacylation of SP-C produces more fluid monolayers at pressures less than 30 mN m-1. The helical secondary structure and tilt angle (70-80 degrees relative to the surface normal) of SP-C remained essentially unchanged upon deacylation in DPPC monolayers at a surface pressure approximately 30 mN m-1. The results are consistent with a model that acylation of SP-C may influence the rapid protein-aided spreading of a surface-associated surfactant reservoir, but not the structure of DPPC or SP-C in the monolayer at higher surface pressures.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
1416
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9889301-1,2-Dipalmitoylphosphatidylcholine,
pubmed-meshheading:9889301-Protein Conformation,
pubmed-meshheading:9889301-Protein Structure, Secondary,
pubmed-meshheading:9889301-Proteolipids,
pubmed-meshheading:9889301-Pulmonary Surfactants,
pubmed-meshheading:9889301-Spectrophotometry, Infrared,
pubmed-meshheading:9889301-Structure-Activity Relationship,
pubmed-meshheading:9889301-Thermodynamics
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pubmed:year |
1999
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pubmed:articleTitle |
Palmitoylation of lung surfactant protein SP-C alters surface thermodynamics, but not protein secondary structure or orientation in 1,2-dipalmitoylphosphatidylcholine langmuir films.
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pubmed:affiliation |
Department of Chemistry, Rutgers University, Newark, NJ 07102, USA. flach@andromeda.rutgers.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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