| pubmed-article:1577735 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0043047 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0023821 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0052181 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0001861 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0001674 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0332261 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C2698172 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C1708533 | lld:lifeskim |
| pubmed-article:1577735 | lifeskim:mentions | umls-concept:C0872351 | lld:lifeskim |
| pubmed-article:1577735 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:1577735 | pubmed:dateCreated | 1992-6-5 | lld:pubmed |
| pubmed-article:1577735 | pubmed:abstractText | The mechanisms that mediate the labile binding of apolipoprotein A-IV (apoA-IV) to high density lipoproteins (HDL) are not known. We therefore used a surface balance and surface radioactivity detector to investigate the adsorption of apoA-IV to egg phosphatidylcholine monolayers spread at the air/water interface. ApoA-IV bound rapidly and reversibly to phospholipid monolayers and generated a maximum increase in surface pressure of 19 millinewtons (mN)/m at a subphase concentration of 2 x 10(-5) g/dl. Binding decreased linearly with increasing initial surface pressure; at pressures greater than 28-29 mN/m, apoA-IV could no longer penetrate the lipid monolayer. The area occupied by the amino acid residues in apoA-IV reached an unusually low limiting molecular area of 10-12 A2/residue at surface saturation. The surface pressure of native HDL3 was calculated to be 33 mN/m, and it rapidly decreased with the action of lecithin:cholesterol acyltransferase on the particle surface. We conclude that the surface activity of apoA-IV is lower than that of any other human apolipoprotein; its binding and surface conformation are particularly sensitive to pressure; and at saturation, a significant portion of the molecule is excluded from the interface. The exclusion pressure of apoA-IV may be only slightly lower than the surface pressure of HDL; in vivo, the action of lecithin:cholesterol acyltransferase and lipid transfer proteins may cause the HDL3 surface pressure to oscillate about a narrow range that spans the exclusion pressure of apoA-IV. The resultant labile association of apoA-IV and HDL may be of central importance to its role in lipoprotein metabolism. | lld:pubmed |
| pubmed-article:1577735 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1577735 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1577735 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1577735 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1577735 | pubmed:month | May | lld:pubmed |
| pubmed-article:1577735 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1577735 | pubmed:author | pubmed-author:PhillipsM CMC | lld:pubmed |
| pubmed-article:1577735 | pubmed:author | pubmed-author:WeinbergR BRB | lld:pubmed |
| pubmed-article:1577735 | pubmed:author | pubmed-author:IbdahJ AJA | lld:pubmed |
| pubmed-article:1577735 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1577735 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1577735 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1577735 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1577735 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1577735 | pubmed:pagination | 8977-83 | lld:pubmed |
| pubmed-article:1577735 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:meshHeading | pubmed-meshheading:1577735-... | lld:pubmed |
| pubmed-article:1577735 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1577735 | pubmed:articleTitle | Adsorption of apolipoprotein A-IV to phospholipid monolayers spread at the air/water interface. A model for its labile binding to high density lipoproteins. | lld:pubmed |
| pubmed-article:1577735 | pubmed:affiliation | Department of Medicine, Bowman Gray School of Medicine, Winston-Salem, North Carolina 27157. | lld:pubmed |
| pubmed-article:1577735 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1577735 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1577735 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1577735 | lld:pubmed |
