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rdf:type |
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lifeskim:mentions |
umls-concept:C0026377,
umls-concept:C0037813,
umls-concept:C0085201,
umls-concept:C0184512,
umls-concept:C0220806,
umls-concept:C0332462,
umls-concept:C0332501,
umls-concept:C0337611,
umls-concept:C1514562,
umls-concept:C1707271,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2603343
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pubmed:issue |
38
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pubmed:dateCreated |
2005-9-19
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pubmed:abstractText |
The structure of apoA-I on discoidal high density lipoprotein (HDL) was studied using a combination of chemical cross-linking and mass spectrometry. Recombinant HDL particles containing 145 molecules of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine and two molecules of apoA-I with a 96-A diameter were treated with the lysine-specific cross-linker, dithiobis(succinimidylpropionate) at varying molar ratios from 2:1 to 200:1. At low molar ratios of dithiobis(succinimidylpropionate) to apoA-I, two products were obtained corresponding to approximately 53 and approximately 80 kDa. At high molar ratios, these two products merged, yielding a product of approximately 59 kDa, close to the theoretical molecular mass of dimeric apoA-I. To identify the intermolecular cross-links giving rise to the two different sized products, bands were excised from the gel, digested with trypsin, and then analyzed by liquid chromatography-electrospray-tandem mass spectrometry. In addition, tandem mass spectrometry of unique cross-links found in the 53- and 80-kDa products suggested that a distinct conformation exists for lipid-bound apoA-I on 96-A recombinant HDL, emphasizing the inherent flexibility and malleability of the N termini and its interaction with its C-terminal domain.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein A-I,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerylphosphorylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Succinimides,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsin,
http://linkedlifedata.com/resource/pubmed/chemical/Urea,
http://linkedlifedata.com/resource/pubmed/chemical/dithiobis(succinimidylpropionate)
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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 |
23
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33015-25
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15972827-Amino Acid Sequence,
pubmed-meshheading:15972827-Apolipoprotein A-I,
pubmed-meshheading:15972827-Chromatography, Liquid,
pubmed-meshheading:15972827-Cross-Linking Reagents,
pubmed-meshheading:15972827-Cysteine,
pubmed-meshheading:15972827-Dimerization,
pubmed-meshheading:15972827-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15972827-Glycerylphosphorylcholine,
pubmed-meshheading:15972827-Lipids,
pubmed-meshheading:15972827-Lysine,
pubmed-meshheading:15972827-Mass Spectrometry,
pubmed-meshheading:15972827-Models, Molecular,
pubmed-meshheading:15972827-Molecular Sequence Data,
pubmed-meshheading:15972827-Mutation,
pubmed-meshheading:15972827-Oligonucleotides,
pubmed-meshheading:15972827-Peptides,
pubmed-meshheading:15972827-Protein Conformation,
pubmed-meshheading:15972827-Protein Denaturation,
pubmed-meshheading:15972827-Protein Folding,
pubmed-meshheading:15972827-Protein Structure, Tertiary,
pubmed-meshheading:15972827-Spectrometry, Mass, Electrospray Ionization,
pubmed-meshheading:15972827-Succinimides,
pubmed-meshheading:15972827-Trypsin,
pubmed-meshheading:15972827-Urea
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pubmed:year |
2005
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pubmed:articleTitle |
Intermolecular contact between globular N-terminal fold and C-terminal domain of ApoA-I stabilizes its lipid-bound conformation: studies employing chemical cross-linking and mass spectrometry.
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pubmed:affiliation |
Pathology and Biochemistry, Wake Forest University Health Sciences, Winston-Salem, North Carolina 27157, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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