rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1980-3-17
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pubmed:abstractText |
The technique of fluorescence recovery after photobleaching was used to investigate the lateral mobility of a fluorescein-labeled amphipathic apolipoprotein, ApoC-III, bound to multibilayers prepared from dipalmitoyl phosphatidylcholine, egg phosphatidylcholine, and a 1:1 (molar ratio) mixture of egg phosphatidylcholine and cholesterol. In dipalmitoyl phosphatidylcholine bilayers the lateral diffusion coefficient (D) for the protein is about 2 x 10(-9) cm(2) sec(-1) at 20 degrees C and about 9 x 10(-8) cm(2) sec(-1) at 45 degrees C. Plots of D versus temperature in this system show a transition between about 30 and 35 degrees C. Arrhenius activation energies for the diffusion in this case between 15 and 30 degrees C and between 35 and 45 degrees C are 28.5 and 7.0 kcal mol(-1), respectively (1 calorie = 4.18 joules). In egg phosphatidylcholine bilayers, D is about 3 x 10(-8) cm(2) sec(-1) at 20 degrees C and the Arrhenius activation energy for diffusion is 8.1 kcal mol(-1) between 15 and 35 degrees C in this system. In bilayers prepared from an equimolar mixture of egg phosphatidylcholine and cholesterol D at 20 degrees C is about 1.4 x 10(-9) cm(2) sec(-1) and the Arrhenius activation energy for the diffusion of the protein in this system between 15 and 35 degrees C is 15.1 kcal mol(-1). Light-scattering and fluorescence-polarization results indicate that binding of this protein does not affect the gel-to-liquid crystalline phase transition of bilayer membranes but does mediate a major, reversible aggregation of the vesicles at about 33 degrees C. These results lend support to the view that ApoC-III resides in the head-group region of the bilayer and suggest that its lateral diffusion coefficient represents an upper bound for integral membrane proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/293667-1004593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/293667-1059096,
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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 |
Nov
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
76
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5645-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:293667-Apolipoproteins,
pubmed-meshheading:293667-Cholesterol,
pubmed-meshheading:293667-Diffusion,
pubmed-meshheading:293667-Lipid Bilayers,
pubmed-meshheading:293667-Membrane Fluidity,
pubmed-meshheading:293667-Membrane Lipids,
pubmed-meshheading:293667-Phosphatidylcholines,
pubmed-meshheading:293667-Photochemistry,
pubmed-meshheading:293667-Solubility,
pubmed-meshheading:293667-Spectrometry, Fluorescence,
pubmed-meshheading:293667-Temperature
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pubmed:year |
1979
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pubmed:articleTitle |
Lateral mobility of an amphipathic apolipoprotein, ApoC-III, bound to phosphatidylcholine bilayers with and without cholesterol.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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