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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1995-3-27
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pubmed:abstractText |
In contrast to the horse heart apocytochrome c, the chicken heart apocytochrome c underwent a conformational change from random coil to partial folding during a renaturation process. When the apocytochrome horse heart and that of chicken heart c were subjected to a translocation assay in vitro using large trypsin-enclosed unilamellar vesicles from soybean phospholipids, the ability of the chicken heart apocytochrome c to penetrate into the liposomes was found to decrease markedly with the renaturation procedure, while that of horse heart apocytochrome c remained relatively constant. Observations from circular dichroism measurement on the induction of secondary folding of these two species of apocytochrome c upon interaction with soybean phospholipid vesicles suggested that a more flexible structure of apocytochrome c embedded in the lipid matrix be required for its efficient translocation across the bilayer.
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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/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c,
http://linkedlifedata.com/resource/pubmed/chemical/Lipid Bilayers,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1001-652X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1341-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7865125-Amino Acid Sequence,
pubmed-meshheading:7865125-Animals,
pubmed-meshheading:7865125-Apoproteins,
pubmed-meshheading:7865125-Chickens,
pubmed-meshheading:7865125-Cytochrome c Group,
pubmed-meshheading:7865125-Cytochromes c,
pubmed-meshheading:7865125-Horses,
pubmed-meshheading:7865125-Lipid Bilayers,
pubmed-meshheading:7865125-Molecular Sequence Data,
pubmed-meshheading:7865125-Nucleic Acid Renaturation,
pubmed-meshheading:7865125-Phospholipids,
pubmed-meshheading:7865125-Protein Folding
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pubmed:year |
1994
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pubmed:articleTitle |
Correlation between unfolded states of apocytochrome c and its ability to pass lipid bilayer.
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pubmed:affiliation |
National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, PRC.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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