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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1986-7-15
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pubmed:abstractText |
Band 3, isolated from human erythrocytes, has been reconstituted into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) deuterated in the terminal methyl groups of the choline head group. By use of Triton X-100 for selective extraction and purification of band 3 and then cholate for subsequent solubilization with the lipid, a number of reconstituted complexes were produced by exhaustive detergent dialysis with protein:lipid weight ratios of between 0.32:1 and 1.25:1. Electron micrographs of negatively stained complexes showed that this method produced large vesicles of greater than 300-nm diameter. Deuterium nuclear magnetic resonance (NMR) spectra from the choline methyl deuterons in bilayer lipid above the liquid-crystal-gel phase transition temperature were shown to change systematically with increasing concentrations of band 3 in the bilayers. The measured quadrupole splittings, taken as the separation of the turning points in the recorded spectra, decreased from a value of 1.28 kHz for pure lipid to 0.98 kHz for bilayers with a protein:lipid ratio of 1.25:1 at 26 degrees C. At 35 degrees C, a more pronounced decrease in the quadrupole splittings was measured. The data from the complexes with protein:lipid ratios up to 0.7:1 (w/w) obey the mathematical treatment for a rapid two-site exchange between lipids at the protein-lipid interface and the bulk lipid phase. The temperature dependence of the measured quadrupole splitting with respect to the protein:lipid ratio indicates that the amount of lipid at the protein-lipid interface increases with increasing temperature.(ABSTRACT TRUNCATED AT 250 WORDS)
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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/Anion Exchange Protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Deuterium,
http://linkedlifedata.com/resource/pubmed/chemical/Dimyristoylphosphatidylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2180-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3707939-Anion Exchange Protein 1, Erythrocyte,
pubmed-meshheading:3707939-Deuterium,
pubmed-meshheading:3707939-Dimyristoylphosphatidylcholine,
pubmed-meshheading:3707939-Humans,
pubmed-meshheading:3707939-Kinetics,
pubmed-meshheading:3707939-Lipid Bilayers,
pubmed-meshheading:3707939-Macromolecular Substances,
pubmed-meshheading:3707939-Magnetic Resonance Spectroscopy,
pubmed-meshheading:3707939-Microscopy, Electron,
pubmed-meshheading:3707939-Thermodynamics
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pubmed:year |
1986
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pubmed:articleTitle |
Evidence from deuterium nuclear magnetic resonance for the temperature-dependent reversible self-association of erythrocyte band 3 in dimyristoylphosphatidylcholine bilayers.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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