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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
1975-12-11
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pubmed:abstractText |
The binding of apoA-I to lysolecithin has been studied by fluorescence and circular dichroism. The influence of the conformation of apoA-I on its interaction with lysolecithin has also been evaluated. ApoA-I is bound to lysolecithin with an association greater than 10(7) whether apoA-I is native or highly unfolded in 1.8 M guanidinium hydrochloride. The association of apoA-I with lysolecithin results in an increase in secondary structure. A 25-residue fragment of apoA-I binds to lysolecithin equally strongly as the native molecule.
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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 |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
250
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7300-6
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:170259-Apoproteins,
pubmed-meshheading:170259-Binding Sites,
pubmed-meshheading:170259-Circular Dichroism,
pubmed-meshheading:170259-Guanidines,
pubmed-meshheading:170259-Humans,
pubmed-meshheading:170259-Kinetics,
pubmed-meshheading:170259-Lipoproteins, HDL,
pubmed-meshheading:170259-Lysophosphatidylcholines,
pubmed-meshheading:170259-Mathematics,
pubmed-meshheading:170259-Protein Binding,
pubmed-meshheading:170259-Protein Conformation,
pubmed-meshheading:170259-Spectrometry, Fluorescence,
pubmed-meshheading:170259-Spectrophotometry, Ultraviolet,
pubmed-meshheading:170259-Succinates
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pubmed:year |
1975
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pubmed:articleTitle |
The interaction of apoA-I from human high density lipoprotein with lysolecithin.
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pubmed:publicationType |
Journal Article
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