| pubmed-article:9521692 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C0205666 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:9521692 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9521692 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:9521692 | pubmed:dateCreated | 1998-4-14 | lld:pubmed |
| pubmed-article:9521692 | pubmed:abstractText | The structural organization and stability of apoB100 in complexes containing triglyceride (TG) and phospholipid have been examined. LDL was delipidated to form aqueous soluble apoB100-TG complexes that retain approximately 70% of LDL TG, but contain no other lipids. The apoB100-TG complexes exhibited reduced amphipathic alpha-helical content (17%) and net negative charge (-2.9 mV) as compared to native LDL-apoB100 (49% and -6 mV, respectively). Of 28 anti-apoB monoclonal antibodies tested, 15 showed partial or full reactivity with apoB100-TG. The immunoreactive epitopes of apoB100-TG were restricted to those situated in either the amino terminal globular domain (4 of 6) or in regions of apoB100 that are predicted to be composed of amphipathic beta-strands (11 of 13). Incubation of the apoB100-TG complex with palmitoyloleoylphosphatidylcholine (POPC) spontaneously (< 10 min) formed homogeneous lipoproteins (20 nm) that contained approximately 300 molecules of POPC per particle (apoB100-PC). Phospholipidation of apoB100-TG complexes partially recovered the alpha-helical content (34%) and net negative charge (-4.9 mV) of the native LDL and restored resistance of apoB100 to denaturation by guanidine HCl (5.8 M). Addition of phospholipids to apoB100-TG also increased the immunoreactivity of specific epitopes that are located primarily in regions of apoB100 that are thought to be constituted of amphipathic beta-strands. The effects of TG and phospholipid on apoB100 conformation appear to be highly domain-specific. On the basis of these results, we propose that the beta-strands of apoB100 may represent a nonflexible lipid-associating backbone, while the amphipathic alpha-helical domains may represent flexible lipid-binding regions that allow the particle to accommodate varying amounts of lipid. | lld:pubmed |
| pubmed-article:9521692 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9521692 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9521692 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9521692 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9521692 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:9521692 | pubmed:author | pubmed-author:SparksD LDL | lld:pubmed |
| pubmed-article:9521692 | pubmed:author | pubmed-author:MilneR WRW | lld:pubmed |
| pubmed-article:9521692 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
| pubmed-article:9521692 | pubmed:author | pubmed-author:ChauhanVV | lld:pubmed |
| pubmed-article:9521692 | pubmed:author | pubmed-author:RamsamyTT | lld:pubmed |
| pubmed-article:9521692 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9521692 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:9521692 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:9521692 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9521692 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9521692 | pubmed:pagination | 3735-42 | lld:pubmed |
| pubmed-article:9521692 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:9521692 | pubmed:meshHeading | pubmed-meshheading:9521692-... | lld:pubmed |
| pubmed-article:9521692 | pubmed:meshHeading | pubmed-meshheading:9521692-... | lld:pubmed |
| pubmed-article:9521692 | pubmed:meshHeading | pubmed-meshheading:9521692-... | lld:pubmed |
| pubmed-article:9521692 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9521692 | pubmed:articleTitle | Evidence for lipid-dependent structural changes in specific domains of apolipoprotein B100. | lld:pubmed |
| pubmed-article:9521692 | pubmed:affiliation | Lipoprotein and Atherosclerosis Group, University of Ottawa Heart Institute, Ontario, Canada. | lld:pubmed |
| pubmed-article:9521692 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9521692 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9521692 | lld:pubmed |
